1M21

Crystal structure analysis of the peptide amidase PAM in complex with the competitive inhibitor chymostatin

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family 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)
A	d1m21a_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Peptide amidase Pam	(Stenotrophomonas maltophilia ) [TaxId: 40324 ],	SCOPe (2.08)
B	d1m21b_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Peptide amidase Pam	(Stenotrophomonas maltophilia ) [TaxId: 40324 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Amidase signature (AS) enzymes	8030840	4002446	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Amidase signature (AS) enzymes	8043219	3001251	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043219	3001251	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	PF01425	e1m21A1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: PF01425	ECOD (1.6)
B	PF01425	e1m21B1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: PF01425	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
B	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01425	Amidase (Amidase)	Amidase	-	Family

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A, B	IPR023631	Amidase signature domain	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	peptide amidase M-CSA #726	Peptide amidase (PAM) from Strenotrophomonas maltophilia (a gram-negative bacterium) catalyses the hydrolysis of the C-terminal amide bond in peptide amides. It is very regio-selective, and those terminal bonds in amino acid side chains are not hydrolysed. PAM belongs to the amidase signature (AS) family, most of which display hydrolase activity. The natural function of periplasmatic PAM is not known.	Defined by 3 residues: LYS:A-86 [auth A-123]SER:A-165 [auth A-202]SER:A-189 [auth A-226] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.1 (PDB Primary Data) Search M-CSA Motif + EC 3.5.1

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.