3OI9

Crystal structure of molybdenum cofactor synthesis domain from Mycobacterium avium

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3oi9a_	Alpha and beta proteins (a/b)	Molybdenum cofactor biosynthesis proteins	Molybdenum cofactor biosynthesis proteins	automated matches	automated matches	(Mycobacterium avium 104 ) [TaxId: 243243 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	MogA-like	8076170	4000598	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Molybdenum cofactor biosynthesis proteins	8076171	3000702	SCOP2 (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	MoCF_biosynth	e3oi9A1	A: a/b three-layered sandwiches	X: Molybdenum cofactor biosynthesis proteins (From Topology)	H: Molybdenum cofactor biosynthesis proteins (From Topology)	T: Molybdenum cofactor biosynthesis proteins	F: MoCF_biosynth	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.980.10	Alpha Beta	3-Layer(aba) Sandwich	Molybdenum Cofactor Biosythetic Enzyme	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00994	Probable molybdopterin binding domain (MoCF_biosynth)	Probable molybdopterin binding domain	This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyr ...	This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Molybdenum cofactor synthesis domain	-	Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process phosphorus metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR051920	Molybdopterin Adenylyltransferase/MoaC-Related	Family
A	IPR036425	MoaB/Mog-like domain superfamily	Homologous Superfamily
A	IPR001453	MoaB/Mog domain	Domain

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.