1RTQ

The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica

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	6
Details	BINDING SITE FOR RESIDUE SCN A 1973

Chain	Residue
A	THR194
A	SER199
A	THR202
A	GLN203
A	LEU262
A	HOH1061

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SCN A 1974

Chain	Residue
A	GLN16
A	ASN135
A	HOH1100
A	HOH1161
A	ALA8
A	ALA12
A	TRP13

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 701

Chain	Residue
A	ASP117
A	GLU152
A	HIS256
A	ZN702
A	HOH1095
A	HOH1189

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 702

Chain	Residue
A	HIS97
A	ASP117
A	ASP179
A	ZN701
A	HOH1095

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site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 703

Chain	Residue
A	TYR218
A	HOH1024
A	HOH1025
A	HOH1026
A	HOH1028
A	HOH1096

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 704

Chain	Residue
A	SER51
A	ASN74
A	HOH1046
A	HOH1048
A	HOH1086
A	HOH1142

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site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 705

Chain	Residue
A	THR268
A	SER270
A	HOH1073
A	HOH1087
A	HOH1090
A	HOH1133

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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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