2HPO

Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1250

Chain	Residue
A	HIS297
A	HIS301
A	GLU320
A	HOH1272

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1270

Chain	Residue
A	HOH1555
A	HOH2105
A	HOH2239
A	ASP58
A	LEU59
A	GLU97
A	ILE98
A	SER99

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1271

Chain	Residue
A	LEU532
A	TRP546
A	SER563
A	ASP566
A	ALA567
A	SER570
A	HOH1948
A	HOH2048

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Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW

Chain	Residue	Details
A	VAL294-TRP303

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865

Chain	Residue	Details
A	TYR299

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	ALA122
A	ALA262
A	GLU298
A	ASN302
A	GLY321

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305

Chain	Residue	Details
A	GLU382

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