2IQ6

Crystal Structure of the Aminopeptidase from Vibrio proteolyticus in Complexation with Leucyl-leucyl-leucine.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008235	molecular_function	metalloexopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 292

Chain	Residue
A	ASP117
A	GLU152
A	HIS256
A	ZN293
B	LEU294

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 293

Chain	Residue
A	ZN292
B	LEU294
A	HIS97
A	ASP117
A	ASP118
A	ASP179

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9

Chain	Residue	Details
A	HIS97
A	ASP117
A	GLU152
A	ASP179
A	HIS256

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1amp

Chain	Residue	Details
A	GLU151

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 167

Chain	Residue	Details
A	HIS97	metal ligand
A	ASP117	metal ligand
A	GLU151	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU152	metal ligand
A	ASP179	metal ligand
A	HIS256	metal ligand

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