5UZ0

Crystal structure of AICARFT bound to an antifolate

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5uz0a1	Alpha and beta proteins (a/b)	Methylglyoxal synthase-like	Methylglyoxal synthase-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d5uz0a2	Alpha and beta proteins (a/b)	Cytidine deaminase-like	Cytidine deaminase-like	AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d5uz0b1	Alpha and beta proteins (a/b)	Methylglyoxal synthase-like	Methylglyoxal synthase-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d5uz0b2	Alpha and beta proteins (a/b)	Cytidine deaminase-like	Cytidine deaminase-like	AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d5uz0c1	Alpha and beta proteins (a/b)	Methylglyoxal synthase-like	Methylglyoxal synthase-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d5uz0c2	Alpha and beta proteins (a/b)	Cytidine deaminase-like	Cytidine deaminase-like	AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d5uz0d1	Alpha and beta proteins (a/b)	Methylglyoxal synthase-like	Methylglyoxal synthase-like	automated matches	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d5uz0d2	Alpha and beta proteins (a/b)	Cytidine deaminase-like	Cytidine deaminase-like	AICAR transformylase domain of bifunctional purine biosynthesis enzyme ATIC	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Methylglyoxal synthase-like	8038873	3001443	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cytidine deaminase-like	8038874	3001838	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cytidine deaminase-like	8038874	3001838	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Methylglyoxal synthase-like	8038873	3001443	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cytidine deaminase-like	8038874	3001838	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Methylglyoxal synthase-like	8038873	3001443	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cytidine deaminase-like	8038874	3001838	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Methylglyoxal synthase-like	8038873	3001443	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	AICARFT_IMPCHas_1st	e5uz0A3	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_1st	ECOD (1.6)
A	AICARFT_IMPCHas_2nd	e5uz0A2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_2nd	ECOD (1.6)
A	MGS	e5uz0A1	A: a/b three-layered sandwiches	X: Methylglyoxal synthase-like (From Topology)	H: Methylglyoxal synthase-like (From Topology)	T: Methylglyoxal synthase-like	F: MGS	ECOD (1.6)
B	AICARFT_IMPCHas_1st	e5uz0B3	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_1st	ECOD (1.6)
B	AICARFT_IMPCHas_2nd	e5uz0B1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_2nd	ECOD (1.6)
B	MGS	e5uz0B2	A: a/b three-layered sandwiches	X: Methylglyoxal synthase-like (From Topology)	H: Methylglyoxal synthase-like (From Topology)	T: Methylglyoxal synthase-like	F: MGS	ECOD (1.6)
C	AICARFT_IMPCHas_1st	e5uz0C3	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_1st	ECOD (1.6)
C	AICARFT_IMPCHas_2nd	e5uz0C1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_2nd	ECOD (1.6)
C	MGS	e5uz0C2	A: a/b three-layered sandwiches	X: Methylglyoxal synthase-like (From Topology)	H: Methylglyoxal synthase-like (From Topology)	T: Methylglyoxal synthase-like	F: MGS	ECOD (1.6)
D	AICARFT_IMPCHas_1st	e5uz0D3	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_1st	ECOD (1.6)
D	AICARFT_IMPCHas_2nd	e5uz0D2	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: AICARFT_IMPCHas_2nd	ECOD (1.6)
D	MGS	e5uz0D1	A: a/b three-layered sandwiches	X: Methylglyoxal synthase-like (From Topology)	H: Methylglyoxal synthase-like (From Topology)	T: Methylglyoxal synthase-like	F: MGS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1380	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Methylglyoxal synthase-like domain	CATH (4.3.0)
A	3.40.140.20	Alpha Beta	3-Layer(aba) Sandwich	Cytidine Deaminase	domain 2	CATH (4.3.0)
A	1.10.287.440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
B	3.40.50.1380	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Methylglyoxal synthase-like domain	CATH (4.3.0)
B	3.40.140.20	Alpha Beta	3-Layer(aba) Sandwich	Cytidine Deaminase	domain 2	CATH (4.3.0)
B	1.10.287.440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
C	3.40.50.1380	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Methylglyoxal synthase-like domain	CATH (4.3.0)
C	3.40.140.20	Alpha Beta	3-Layer(aba) Sandwich	Cytidine Deaminase	domain 2	CATH (4.3.0)
C	1.10.287.440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
D	3.40.50.1380	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Methylglyoxal synthase-like domain	CATH (4.3.0)
D	3.40.140.20	Alpha Beta	3-Layer(aba) Sandwich	Cytidine Deaminase	domain 2	CATH (4.3.0)
D	1.10.287.440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02142	MGS-like domain (MGS)	MGS-like domain	This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes ino ...	This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site [1].	Domain
A, B, C, D	PF01808	AICARFT/IMPCHase bienzyme (AICARFT_IMPCHas)	AICARFT/IMPCHase bienzyme	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Bifunctional purine biosynthesis protein PURH	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines IMP cyclohydrolase activity cyclohydrolase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds phosphoribosylaminoimidazolecarboxamide formyltransferase activity transferase activity, transferring one-carbon groups transferase activity hydroxymethyl-, formyl- and related transferase activity identical protein binding protein binding binding protein homodimerization activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines IMP cyclohydrolase activity cyclohydrolase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds phosphoribosylaminoimidazolecarboxamide formyltransferase activity transferase activity, transferring one-carbon groups transferase activity hydroxymethyl-, formyl- and related transferase activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity cell adhesion molecule binding cadherin binding	developmental process anatomical structure development brainstem development ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process developmental process anatomical structure development brainstem development ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process purine nucleoside monophosphate metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process purine-containing compound metabolic process IMP biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process 'de novo' IMP biosynthetic process purine ribonucleotide metabolic process ribonucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process 'de novo' AMP biosynthetic process AMP metabolic process AMP biosynthetic process GMP metabolic process GMP biosynthetic process 'de novo' XMP biosynthetic process XMP metabolic process XMP biosynthetic process multicellular organismal process head development animal organ development brain development nervous system development multicellular organism development cerebellum development central nervous system development metencephalon development hindbrain development system development forebrain development pallium development cerebral cortex development telencephalon development oxoacid metabolic process dicarboxylic acid metabolic process dihydrofolate metabolic process carboxylic acid metabolic process modified amino acid metabolic process organic acid metabolic process folic acid-containing compound metabolic process pteridine-containing compound metabolic process animal organ regeneration regeneration folic acid-containing compound biosynthetic process modified amino acid biosynthetic process pteridine-containing compound biosynthetic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process response to peptide response to interleukin-7 response to stimulus response to chemical response to cytokine cellular response to cytokine stimulus cellular response to interleukin-7	cellular anatomical structure membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cellular anatomical structure membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR011607	Methylglyoxal synthase-like domain	Domain
A, B, C, D	IPR002695	Bifunctional purine biosynthesis protein PurH-like	Family
A, B, C, D	IPR024051	AICAR transformylase, duplicated domain superfamily	Homologous Superfamily
A, B, C, D	IPR036914	Methylglyoxal synthase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR016193	Cytidine deaminase-like	Homologous Superfamily
A, B, C, D	IPR024050	AICAR transformylase, insert domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P31939	AICA-ribosiduria rheumatoid arthritis osteoporosis epilepsy heart disease large cell medulloblastoma Malignant tumor of lung acute lymphoblastic leukemia mycosis fungoides non-small cell lung carcinoma blindness (disorder) plasma cell myeloma psoriatic arthritis intellectual disability lung cancer AICA-ribosiduria rheumatoid arthritis osteoporosis epilepsy heart disease large cell medulloblastoma Malignant tumor of lung acute lymphoblastic leukemia mycosis fungoides non-small cell lung carcinoma blindness (disorder) plasma cell myeloma psoriatic arthritis intellectual disability lung cancer medulloblastoma myocardial infarction astrocytic tumor ovarian cancer bone osteosarcoma diabetes mellitus endometriosis gestational trophoblastic neoplasm juvenile idiopathic arthritis psoriasis Burkitt lymphoma

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.