3PZY

Crystal structure of Molybdopterin biosynthesis mog protein from Mycobacterium paratuberculosis

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	d3pzya_	Alpha and beta proteins (a/b)	Molybdenum cofactor biosynthesis proteins	Molybdenum cofactor biosynthesis proteins	automated matches	automated matches	(Mycobacterium avium subsp. paratuberculosis ) [TaxId: 1770 ],	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	8076172	4000598	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Molybdenum cofactor biosynthesis proteins	8076173	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	e3pzyA1	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	Mog	-	Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor 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 Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor 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.