3B3W

Crystal structure of the S228A mutant of the aminopeptidase from Vibrio proteolyticus in complex with 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	4
Details	BINDING SITE FOR RESIDUE ZN A 292

Chain	Residue
A	ASP117
A	GLU152
A	HIS256
A	LEU297

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 293

Chain	Residue
A	HIS97
A	ASP117
A	ASP179
A	LEU297

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SCN A 294

Chain	Residue
A	SER199
A	THR202
A	GLN203
A	PRO267
A	HOH506
A	THR194

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 295

Chain	Residue
A	TYR218
A	NA296
A	HOH347
A	HOH348
A	HOH387
A	HOH502

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site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NA A 296

Chain	Residue
A	THR206
A	ASP210
A	TYR218
A	NA295
A	HOH310
A	HOH347
A	HOH387
A	HOH502

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site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LEU A 297

Chain	Residue
A	HIS97
A	ASP117
A	GLU151
A	GLU152
A	ASP179
A	TYR225
A	CYS227
A	HIS256
A	ZN292
A	ZN293
A	HOH360

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10413478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11401547","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8087555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8647077","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AMP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CP6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FT7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IGB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LOK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RTQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XRY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ANP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IQ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NYQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B3W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VH9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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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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