4HG3

Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Carbon-nitrogen hydrolases	8081714	3001086	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Carbon-nitrogen hydrolases	8081714	3001086	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Carbon-nitrogen hydrolases	8081714	3001086	SCOP2B (2022-06-29)
D	SCOP2 Family	Carbon-nitrogen hydrolases-like	8081713	4002312	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	Carbon-nitrogen hydrolases	8081714	3001086	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	PF00795	e4hg3A1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: PF00795	ECOD (1.6)
B	PF00795	e4hg3B1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: PF00795	ECOD (1.6)
C	PF00795	e4hg3C1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: PF00795	ECOD (1.6)
D	PF00795	e4hg3D1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: PF00795	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
B	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
C	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
D	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00795	Carbon-nitrogen hydrolase (CN_hydrolase)	Carbon-nitrogen hydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Probable hydrolase NIT2	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides deaminated glutathione amidase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds phosphoric ester hydrolase activity phosphoprotein phosphatase activity [acetyl-CoA carboxylase]-phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds phosphatase activity	catabolic process amide catabolic process metabolic process amide metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036526	Carbon-nitrogen hydrolase superfamily	Homologous Superfamily
A, B, C, D	IPR045254	Nit1/2, carbon-nitrogen hydrolase domain	Domain
A, B, C, D	IPR003010	Carbon-nitrogen hydrolase	Domain
A, B, C, D	IPR001110	Uncharacterised protein family UPF0012, conserved site	Conserved Site

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 R01GM133198.