Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1W2M

Ca-substituted form of E. coli aminopeptidase P

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	0008235	molecular_function	metalloexopeptidase activity
A	0008237	molecular_function	metallopeptidase 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	0008235	molecular_function	metalloexopeptidase activity
B	0008237	molecular_function	metallopeptidase 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	0008235	molecular_function	metalloexopeptidase activity
C	0008237	molecular_function	metallopeptidase 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	0008235	molecular_function	metalloexopeptidase activity
D	0008237	molecular_function	metallopeptidase 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	0008235	molecular_function	metalloexopeptidase activity
E	0008237	molecular_function	metallopeptidase 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	0008235	molecular_function	metalloexopeptidase activity
F	0008237	molecular_function	metallopeptidase 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	4
Details	BINDING SITE FOR RESIDUE IPA A 1440

Chain	Residue
A	ILE27
A	PHE28
A	TRP165
A	HOH2013

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA A 1441

Chain	Residue
B	MET162
A	ARG149
A	PRO159
A	ALA160
A	THR161
A	HOH2177

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 1442

Chain	Residue
A	ASP271
A	HIS354
A	GLU383
A	GLU406
A	HOH2163

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1443

Chain	Residue
A	ARG79
A	VAL80
A	PHE110
A	SER111

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 1439

Chain	Residue
B	ILE27
B	PHE28
B	TRP165
B	HOH2054

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA B 1440

Chain	Residue
A	MET162
A	HOH2064
B	ARG149
B	PRO159
B	ALA160

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 1441

Chain	Residue
B	ASP271
B	HIS354
B	GLU383
B	GLU406
B	HOH2136

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 1442

Chain	Residue
B	ARG79
B	VAL80
B	PHE110
B	SER111

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA C 1440

Chain	Residue
C	ILE27
C	PHE28
C	ASN46
C	TRP165
C	HOH2015

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 1441

Chain	Residue
C	ASP271
C	HIS354
C	GLU383
C	GLU406
C	HOH2140
C	HOH2143

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 1442

Chain	Residue
C	VAL80
C	PHE110
C	SER111

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPA D 1441

Chain	Residue
C	ARG149
C	PRO159
C	ALA160
D	MET162
D	ASP164
D	HOH2178

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA D 1442

Chain	Residue
D	ILE27
D	PHE28
D	ASN46
D	TRP165
D	HOH2015

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA D 1443

Chain	Residue
C	MET162
D	ARG149
D	PRO159
D	ALA160
D	HOH2179

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 1444

Chain	Residue
D	ASP271
D	HIS354
D	GLU383
D	GLU406
D	HOH2157

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 1445

Chain	Residue
D	ARG79
D	VAL80
D	PHE110
D	SER111

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA E 1440

Chain	Residue
E	ILE27
E	PHE28
E	TRP165
E	HOH2024

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA E 1441

Chain	Residue
E	ARG149
E	PRO159
E	ALA160
E	HOH2222
F	MET162

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 1442

Chain	Residue
E	ASP271
E	HIS354
E	GLU383
E	GLU406
E	HOH2183
E	HOH2204

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 1443

Chain	Residue
E	VAL80
E	PHE110
E	SER111

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA F 1441

Chain	Residue
F	ILE27
F	PHE28
F	ASN46
F	TRP165
F	HOH2189

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA F 1442

Chain	Residue
E	MET162
F	ARG149
F	PRO159
F	ALA160
F	HOH2190

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 1443

Chain	Residue
F	ASP271
F	HIS354
F	GLU383
F	GLU406
F	HOH2172

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL F 1444

Chain	Residue
F	ARG79
F	VAL80
F	PHE110
F	SER111

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:

Chain	Residue	Details
A	ALA261
B	ASP407
C	ALA261
C	ILE272
C	TRP355
C	PRO384
C	ASP407
D	ALA261
D	ILE272
D	TRP355
D	PRO384
A	ILE272
D	ASP407
E	ALA261
E	ILE272
E	TRP355
E	PRO384
E	ASP407
F	ALA261
F	ILE272
F	TRP355
F	PRO384
A	TRP355
F	ASP407
A	PRO384
A	ASP407
B	ALA261
B	ILE272
B	TRP355
B	PRO384

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	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	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	MCSA1
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
A	SER39	activator, electrostatic stabiliser
A	ILE405	proton shuttle (general acid/base)
A	ASP407	metal ligand
A	TYR244	electrostatic stabiliser
A	ALA261	metal ligand, proton shuttle (general acid/base)
A	ILE272	metal ligand
A	GLY351	electrostatic stabiliser
A	TRP355	metal ligand
A	ASP362	electrostatic stabiliser
A	PRO384	activator, metal ligand, proton shuttle (general acid/base)
A	ILE388	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
B	SER39	activator, electrostatic stabiliser
B	ILE405	proton shuttle (general acid/base)
B	ASP407	metal ligand
B	TYR244	electrostatic stabiliser
B	ALA261	metal ligand, proton shuttle (general acid/base)
B	ILE272	metal ligand
B	GLY351	electrostatic stabiliser
B	TRP355	metal ligand
B	ASP362	electrostatic stabiliser
B	PRO384	activator, metal ligand, proton shuttle (general acid/base)
B	ILE388	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
C	SER39	activator, electrostatic stabiliser
C	ILE405	proton shuttle (general acid/base)
C	ASP407	metal ligand
C	TYR244	electrostatic stabiliser
C	ALA261	metal ligand, proton shuttle (general acid/base)
C	ILE272	metal ligand
C	GLY351	electrostatic stabiliser
C	TRP355	metal ligand
C	ASP362	electrostatic stabiliser
C	PRO384	activator, metal ligand, proton shuttle (general acid/base)
C	ILE388	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
D	SER39	activator, electrostatic stabiliser
D	ILE405	proton shuttle (general acid/base)
D	ASP407	metal ligand
D	TYR244	electrostatic stabiliser
D	ALA261	metal ligand, proton shuttle (general acid/base)
D	ILE272	metal ligand
D	GLY351	electrostatic stabiliser
D	TRP355	metal ligand
D	ASP362	electrostatic stabiliser
D	PRO384	activator, metal ligand, proton shuttle (general acid/base)
D	ILE388	proton shuttle (general acid/base)

site_id	MCSA5
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
E	SER39	activator, electrostatic stabiliser
E	ILE405	proton shuttle (general acid/base)
E	ASP407	metal ligand
E	TYR244	electrostatic stabiliser
E	ALA261	metal ligand, proton shuttle (general acid/base)
E	ILE272	metal ligand
E	GLY351	electrostatic stabiliser
E	TRP355	metal ligand
E	ASP362	electrostatic stabiliser
E	PRO384	activator, metal ligand, proton shuttle (general acid/base)
E	ILE388	proton shuttle (general acid/base)

site_id	MCSA6
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
F	SER39	activator, electrostatic stabiliser
F	ILE405	proton shuttle (general acid/base)
F	ASP407	metal ligand
F	TYR244	electrostatic stabiliser
F	ALA261	metal ligand, proton shuttle (general acid/base)
F	ILE272	metal ligand
F	GLY351	electrostatic stabiliser
F	TRP355	metal ligand
F	ASP362	electrostatic stabiliser
F	PRO384	activator, metal ligand, proton shuttle (general acid/base)
F	ILE388	proton shuttle (general acid/base)

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