Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M35

Aminopeptidase P from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0016787	molecular_function	hydrolase activity
A	0030145	molecular_function	manganese ion binding
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0070006	molecular_function	metalloaminopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008235	molecular_function	metalloexopeptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0016787	molecular_function	hydrolase activity
B	0030145	molecular_function	manganese ion binding
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0070006	molecular_function	metalloaminopeptidase activity
C	0004177	molecular_function	aminopeptidase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008235	molecular_function	metalloexopeptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0016787	molecular_function	hydrolase activity
C	0030145	molecular_function	manganese ion binding
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
C	0070006	molecular_function	metalloaminopeptidase activity
D	0004177	molecular_function	aminopeptidase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008235	molecular_function	metalloexopeptidase activity
D	0008237	molecular_function	metallopeptidase activity
D	0016787	molecular_function	hydrolase activity
D	0030145	molecular_function	manganese ion binding
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization
D	0070006	molecular_function	metalloaminopeptidase activity
E	0004177	molecular_function	aminopeptidase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008235	molecular_function	metalloexopeptidase activity
E	0008237	molecular_function	metallopeptidase activity
E	0016787	molecular_function	hydrolase activity
E	0030145	molecular_function	manganese ion binding
E	0032991	cellular_component	protein-containing complex
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0051289	biological_process	protein homotetramerization
E	0070006	molecular_function	metalloaminopeptidase activity
F	0004177	molecular_function	aminopeptidase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0008235	molecular_function	metalloexopeptidase activity
F	0008237	molecular_function	metallopeptidase activity
F	0016787	molecular_function	hydrolase activity
F	0030145	molecular_function	manganese ion binding
F	0032991	cellular_component	protein-containing complex
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0051289	biological_process	protein homotetramerization
F	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 2001

Chain	Residue
A	ASP260
A	ASP271
A	THR273
A	GLU406
A	MN2002
A	HOH2042
A	HOH2150

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 2002

Chain	Residue
A	GLU383
A	GLU406
A	MN2001
A	HOH2150
A	ASP271
A	HIS354

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN B 2003

Chain	Residue
B	ASP260
B	ASP271
B	THR273
B	GLU406
B	MN2004
B	HOH2202
B	HOH2203

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 2004

Chain	Residue
B	ASP271
B	HIS354
B	GLU383
B	GLU406
B	MN2003
B	HOH2202

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MN C 2005

Chain	Residue
C	TYR229
C	ASP260
C	ASP271
C	THR273
C	GLU406
C	MN2006
C	HOH2049
C	HOH2171

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 2006

Chain	Residue
C	ASP271
C	HIS354
C	GLU383
C	GLU406
C	MN2005
C	HOH2171

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 2007

Chain	Residue
D	ASP260
D	ASP271
D	THR273
D	GLU406
D	MN2008
D	HOH2067
D	HOH2226

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 2008

Chain	Residue
D	ASP271
D	HIS354
D	GLU383
D	GLU406
D	MN2007
D	HOH2226

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MN E 2009

Chain	Residue
E	TYR229
E	ASP260
E	ASP271
E	THR273
E	GLU406
E	HOH614
E	HOH1309
E	MN2010

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN E 2010

Chain	Residue
E	ASP271
E	HIS354
E	GLU383
E	GLU406
E	HOH1309
E	HOH1610
E	MN2009

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MN F 2011

Chain	Residue
F	TYR229
F	ASP260
F	ASP271
F	THR273
F	GLU406
F	HOH766
F	HOH855
F	MN2012

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN F 2012

Chain	Residue
F	ASP271
F	HIS354
F	GLU383
F	GLU406
F	HOH855
F	MN2011

Functional Information from PROSITE/UniProt

site_id	PS00491
Number of Residues	13
Details	PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLSHwLGLdVHD

Chain	Residue	Details
A	HIS350-ASP362

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
A	GLU383
A	HIS361

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
B	GLU383
B	HIS361

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
C	GLU383
C	HIS361

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
D	GLU383
D	HIS361

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
E	GLU383
E	HIS361

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
F	GLU383
F	HIS361

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
A	GLU383

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
B	GLU383

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
C	GLU383

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
D	GLU383

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
E	GLU383

site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
F	GLU383

site_id	MCSA1
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
A	ASP38	activator, electrostatic stabiliser
A	ARG404	proton shuttle (general acid/base)
A	GLU406	metal ligand
A	HIS243	electrostatic stabiliser
A	ASP260	metal ligand, proton shuttle (general acid/base)
A	ASP271	metal ligand
A	HIS350	electrostatic stabiliser
A	HIS354	metal ligand
A	HIS361	electrostatic stabiliser
A	GLU383	activator, metal ligand, proton shuttle (general acid/base)
A	TYR387	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
B	ASP38	activator, electrostatic stabiliser
B	ARG404	proton shuttle (general acid/base)
B	GLU406	metal ligand
B	HIS243	electrostatic stabiliser
B	ASP260	metal ligand, proton shuttle (general acid/base)
B	ASP271	metal ligand
B	HIS350	electrostatic stabiliser
B	HIS354	metal ligand
B	HIS361	electrostatic stabiliser
B	GLU383	activator, metal ligand, proton shuttle (general acid/base)
B	TYR387	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
C	ASP38	activator, electrostatic stabiliser
C	ARG404	proton shuttle (general acid/base)
C	GLU406	metal ligand
C	HIS243	electrostatic stabiliser
C	ASP260	metal ligand, proton shuttle (general acid/base)
C	ASP271	metal ligand
C	HIS350	electrostatic stabiliser
C	HIS354	metal ligand
C	HIS361	electrostatic stabiliser
C	GLU383	activator, metal ligand, proton shuttle (general acid/base)
C	TYR387	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
D	ASP38	activator, electrostatic stabiliser
D	ARG404	proton shuttle (general acid/base)
D	GLU406	metal ligand
D	HIS243	electrostatic stabiliser
D	ASP260	metal ligand, proton shuttle (general acid/base)
D	ASP271	metal ligand
D	HIS350	electrostatic stabiliser
D	HIS354	metal ligand
D	HIS361	electrostatic stabiliser
D	GLU383	activator, metal ligand, proton shuttle (general acid/base)
D	TYR387	proton shuttle (general acid/base)

site_id	MCSA5
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
E	ASP38	activator, electrostatic stabiliser
E	ARG404	proton shuttle (general acid/base)
E	GLU406	metal ligand
E	HIS243	electrostatic stabiliser
E	ASP260	metal ligand, proton shuttle (general acid/base)
E	ASP271	metal ligand
E	HIS350	electrostatic stabiliser
E	HIS354	metal ligand
E	HIS361	electrostatic stabiliser
E	GLU383	activator, metal ligand, proton shuttle (general acid/base)
E	TYR387	proton shuttle (general acid/base)

site_id	MCSA6
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
F	ASP38	activator, electrostatic stabiliser
F	ARG404	proton shuttle (general acid/base)
F	GLU406	metal ligand
F	HIS243	electrostatic stabiliser
F	ASP260	metal ligand, proton shuttle (general acid/base)
F	ASP271	metal ligand
F	HIS350	electrostatic stabiliser
F	HIS354	metal ligand
F	HIS361	electrostatic stabiliser
F	GLU383	activator, metal ligand, proton shuttle (general acid/base)
F	TYR387	proton shuttle (general acid/base)

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)