1LOK

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

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 901

Chain	Residue
A	ASP117
A	GLU152
A	HIS256
A	TRS800
A	ZN902

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 902

Chain	Residue
A	ASP179
A	TRS800
A	ZN901
A	HIS97
A	ASP117
A	GLU151
A	GLU152

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 903

Chain	Residue
A	TYR218
A	HOH1024
A	HOH1035
A	HOH1043
A	HOH1045
A	HOH1095

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SCN A 1973

Chain	Residue
A	ASN171
A	VAL172
A	TYR238
A	PRO239
A	HOH1192

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site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TRS A 800

Chain	Residue
A	HIS97
A	ASP117
A	GLU151
A	GLU152
A	ASP179
A	MET180
A	TYR225
A	CYS227
A	HIS256
A	ZN901
A	ZN902
A	HOH1116
A	HOH1293

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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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