Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1WBQ

ZnMg substituted aminopeptidase P from E. 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A1440

Chain	Residue
A	ASP271
A	HIS354
A	THR381
A	GLU383
A	GLU406
A	MG1441
A	HOH2191

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG A1441

Chain	Residue
A	ASP271
A	THR273
A	GLU406
A	ZN1440
A	HOH2134
A	HOH2191
A	TYR229
A	ASP260

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A1442

Chain	Residue
A	ARG79
A	VAL80
A	SER111

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B1440

Chain	Residue
B	ASP271
B	HIS354
B	THR381
B	GLU383
B	GLU406
B	MG1441
B	HOH2285

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG B1441

Chain	Residue
B	TYR229
B	ASP260
B	ASP271
B	THR273
B	GLU406
B	ZN1440
B	HOH2198
B	HOH2285

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B1442

Chain	Residue
B	HOH2254
B	HOH2255
B	HOH2257
B	HOH2258
D	HOH2155
D	HOH2158

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B1443

Chain	Residue
B	ARG79
B	VAL80
B	SER111

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C1440

Chain	Residue
C	ASP271
C	HIS354
C	THR381
C	GLU383
C	GLU406
C	MG1441

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C1441

Chain	Residue
C	ASP260
C	ASP271
C	THR273
C	GLU406
C	ZN1440

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C1442

Chain	Residue
C	VAL80
C	PHE110
C	SER111

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN D1440

Chain	Residue
D	ASP271
D	HIS354
D	THR381
D	GLU383
D	GLU406
D	MG1441
D	HOH2256

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG D1441

Chain	Residue
D	TYR229
D	ASP260
D	ASP271
D	THR273
D	GLU406
D	ZN1440
D	HOH2172
D	HOH2256

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D1442

Chain	Residue
B	HOH2184
D	HOH2062
D	HOH2225
D	HOH2228
D	HOH2231
D	HOH2232

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D1443

Chain	Residue
D	VAL80
D	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	20
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	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
A	GLU383

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

Chain	Residue	Details
B	GLU383

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

Chain	Residue	Details
C	GLU383

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

Chain	Residue	Details
D	GLU383

site_id	MCSA1
Number of Residues	11
Details	M-CSA 379

Chain	Residue	Details
A	ASP38	activator, electrostatic stabiliser
A	ASP408	proton shuttle (general acid/base)
A	VAL410	metal ligand
A	HIS243	electrostatic stabiliser
A	GLU264	metal ligand, proton shuttle (general acid/base)
A	THR275	metal ligand
A	HIS354	electrostatic stabiliser
A	LEU358	metal ligand
A	VAL365	electrostatic stabiliser
A	TYR387	activator, metal ligand, proton shuttle (general acid/base)
A	ASP391	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	ASP408	proton shuttle (general acid/base)
B	VAL410	metal ligand
B	HIS243	electrostatic stabiliser
B	GLU264	metal ligand, proton shuttle (general acid/base)
B	THR275	metal ligand
B	HIS354	electrostatic stabiliser
B	LEU358	metal ligand
B	VAL365	electrostatic stabiliser
B	TYR387	activator, metal ligand, proton shuttle (general acid/base)
B	ASP391	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	ASP408	proton shuttle (general acid/base)
C	VAL410	metal ligand
C	HIS243	electrostatic stabiliser
C	GLU264	metal ligand, proton shuttle (general acid/base)
C	THR275	metal ligand
C	HIS354	electrostatic stabiliser
C	LEU358	metal ligand
C	VAL365	electrostatic stabiliser
C	TYR387	activator, metal ligand, proton shuttle (general acid/base)
C	ASP391	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	ASP408	proton shuttle (general acid/base)
D	VAL410	metal ligand
D	HIS243	electrostatic stabiliser
D	GLU264	metal ligand, proton shuttle (general acid/base)
D	THR275	metal ligand
D	HIS354	electrostatic stabiliser
D	LEU358	metal ligand
D	VAL365	electrostatic stabiliser
D	TYR387	activator, metal ligand, proton shuttle (general acid/base)
D	ASP391	proton shuttle (general acid/base)

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