1UF7 | pdb_00001uf7

Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1uf7b_	Alpha and beta proteins (a+b)	Carbon-nitrogen hydrolase	Carbon-nitrogen hydrolase	Carbamilase	N-carbamoyl-D-aminoacid amidohydrolase	(Agrobacterium sp. ) [TaxId: 361 ],	SCOPe (2.08)
A	d1uf7a_	Alpha and beta proteins (a+b)	Carbon-nitrogen hydrolase	Carbon-nitrogen hydrolase	Carbamilase	N-carbamoyl-D-aminoacid amidohydrolase	(Agrobacterium sp. ) [TaxId: 361 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Carbon-nitrogen hydrolases	8032819	3001086	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Carbon-nitrogen hydrolases	8032819	3001086	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)
B	CN_hydrolase	e1uf7B1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: CN_hydrolase	ECOD (1.6)
A	CN_hydrolase	e1uf7A1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: CN_hydrolase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
A	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	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	N-carbamyl-D-amino acid amidohydrolase	N-carbamoyl-D-amino acid hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036526	Carbon-nitrogen hydrolase superfamily	Homologous Superfamily
A, B	IPR050345	Aliphatic Amidase/Beta-Ureidopropionase	Family
A, B	IPR003010	Carbon-nitrogen hydrolase	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	N-carbamoyl-D-amino-acid hydrolase M-CSA #674	N-carbomyl-D-amino acid amindohydrolase (DCase) catalyses the hydrolysis of N-carbomyl-D-amino acids to the corresponding D-amino acids, which are useful in preparation of physiologically active peptides and beta-lactam antibiotics.	Defined by 3 residues: GLU:A-46LYS:A-126ALA:A-171 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.1.77 (PDB Primary Data) Search M-CSA Motif + EC 3.5.1.77

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.