Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OV8

2.6 Angstrom Resolution Crystal Structure of Aminopeptidase B from Escherichia coli str. K-12 substr. MG1655

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	0016787	molecular_function	hydrolase activity
A	0019538	biological_process	protein metabolic process
A	0030145	molecular_function	manganese ion binding
A	0042802	molecular_function	identical protein binding
A	0043171	biological_process	peptide catabolic process
A	0046872	molecular_function	metal ion binding
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	0016787	molecular_function	hydrolase activity
B	0019538	biological_process	protein metabolic process
B	0030145	molecular_function	manganese ion binding
B	0042802	molecular_function	identical protein binding
B	0043171	biological_process	peptide catabolic process
B	0046872	molecular_function	metal ion binding
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	0016787	molecular_function	hydrolase activity
C	0019538	biological_process	protein metabolic process
C	0030145	molecular_function	manganese ion binding
C	0042802	molecular_function	identical protein binding
C	0043171	biological_process	peptide catabolic process
C	0046872	molecular_function	metal ion binding
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	0016787	molecular_function	hydrolase activity
D	0019538	biological_process	protein metabolic process
D	0030145	molecular_function	manganese ion binding
D	0042802	molecular_function	identical protein binding
D	0043171	biological_process	peptide catabolic process
D	0046872	molecular_function	metal ion binding
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	0016787	molecular_function	hydrolase activity
E	0019538	biological_process	protein metabolic process
E	0030145	molecular_function	manganese ion binding
E	0042802	molecular_function	identical protein binding
E	0043171	biological_process	peptide catabolic process
E	0046872	molecular_function	metal ion binding
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	0016787	molecular_function	hydrolase activity
F	0019538	biological_process	protein metabolic process
F	0030145	molecular_function	manganese ion binding
F	0042802	molecular_function	identical protein binding
F	0043171	biological_process	peptide catabolic process
F	0046872	molecular_function	metal ion binding
F	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue ZN A 501

Chain	Residue
A	LYS195
A	ASP200
A	ASP218
A	GLU279
A	MN502
A	HOH662

site_id	AC2
Number of Residues	6
Details	binding site for residue MN A 502

Chain	Residue
A	GLU279
A	ZN501
A	HOH662
A	ASP200
A	LYS207
A	ASP277

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 503

Chain	Residue
A	GLY19
A	GLU20
A	LYS21

site_id	AC4
Number of Residues	1
Details	binding site for residue CL A 504

Chain	Residue
A	ALA411

site_id	AC5
Number of Residues	4
Details	binding site for residue CL A 505

Chain	Residue
A	ALA278
A	GLY280
A	ARG281
A	LEU305

site_id	AC6
Number of Residues	3
Details	binding site for residue CL A 506

Chain	Residue
A	ALA80
A	ARG85
A	HOH720

site_id	AC7
Number of Residues	6
Details	binding site for residue ZN B 501

Chain	Residue
B	LYS195
B	ASP200
B	ASP218
B	GLU279
B	MN502
B	HOH693

site_id	AC8
Number of Residues	5
Details	binding site for residue MN B 502

Chain	Residue
B	ASP200
B	ASP277
B	GLU279
B	ZN501
B	HOH693

site_id	AC9
Number of Residues	3
Details	binding site for residue CL B 503

Chain	Residue
B	GLY19
B	GLU20
B	LYS21

site_id	AD1
Number of Residues	4
Details	binding site for residue CL B 504

Chain	Residue
B	ALA278
B	GLY280
B	ARG281
B	HOH686

site_id	AD2
Number of Residues	2
Details	binding site for residue CL B 505

Chain	Residue
B	ALA411
F	HOH669

site_id	AD3
Number of Residues	1
Details	binding site for residue CL B 506

Chain	Residue
B	ARG85

site_id	AD4
Number of Residues	7
Details	binding site for residue ZN C 501

Chain	Residue
C	LYS195
C	ASP200
C	ASP218
C	GLU279
C	MN502
C	HOH681
C	HOH688

site_id	AD5
Number of Residues	5
Details	binding site for residue MN C 502

Chain	Residue
C	ASP200
C	ASP277
C	GLU279
C	ZN501
C	HOH688

site_id	AD6
Number of Residues	4
Details	binding site for residue CL C 503

Chain	Residue
C	ALA278
C	ARG281
C	LEU305
C	HOH681

site_id	AD7
Number of Residues	2
Details	binding site for residue CL C 504

Chain	Residue
C	SER410
C	ALA411

site_id	AD8
Number of Residues	3
Details	binding site for residue CL C 505

Chain	Residue
C	ALA80
C	ARG85
C	HOH675

site_id	AD9
Number of Residues	6
Details	binding site for residue ZN D 501

Chain	Residue
D	LYS195
D	ASP200
D	ASP218
D	GLU279
D	MN502
D	HOH700

site_id	AE1
Number of Residues	5
Details	binding site for residue MN D 502

Chain	Residue
D	ASP200
D	ASP277
D	GLU279
D	ZN501
D	HOH700

site_id	AE2
Number of Residues	4
Details	binding site for residue CL D 503

Chain	Residue
D	ALA278
D	GLY280
D	ARG281
D	LEU305

site_id	AE3
Number of Residues	2
Details	binding site for residue CL D 504

Chain	Residue
B	HOH613
D	ALA411

site_id	AE4
Number of Residues	2
Details	binding site for residue CL D 505

Chain	Residue
D	LEU41
D	ARG70

site_id	AE5
Number of Residues	7
Details	binding site for residue ZN E 501

Chain	Residue
E	LYS195
E	ASP200
E	ASP218
E	GLU279
E	MN502
E	HOH643
E	HOH693

site_id	AE6
Number of Residues	5
Details	binding site for residue MN E 502

Chain	Residue
E	ASP200
E	ASP277
E	GLU279
E	ZN501
E	HOH693

site_id	AE7
Number of Residues	5
Details	binding site for residue CL E 503

Chain	Residue
E	LEU305
E	HOH643
E	ALA278
E	GLY280
E	ARG281

site_id	AE8
Number of Residues	1
Details	binding site for residue CL E 504

Chain	Residue
E	ALA411

site_id	AE9
Number of Residues	1
Details	binding site for residue CL E 505

Chain	Residue
E	ARG85

site_id	AF1
Number of Residues	7
Details	binding site for residue ZN F 501

Chain	Residue
F	LYS195
F	ASP200
F	ASP218
F	GLU279
F	MN502
F	HOH641
F	HOH679

site_id	AF2
Number of Residues	5
Details	binding site for residue MN F 502

Chain	Residue
F	ASP200
F	ASP277
F	GLU279
F	ZN501
F	HOH679

site_id	AF3
Number of Residues	5
Details	binding site for residue CL F 503

Chain	Residue
F	ALA278
F	GLY280
F	ARG281
F	LEU305
F	HOH641

site_id	AF4
Number of Residues	1
Details	binding site for residue CL F 504

Chain	Residue
F	ALA411

site_id	AF5
Number of Residues	1
Details	binding site for residue CL F 505

Chain	Residue
F	ARG85

site_id	AF6
Number of Residues	1
Details	binding site for residue CL F 506

Chain	Residue
F	ASN238

Functional Information from PROSITE/UniProt

site_id	PS00631
Number of Residues	8
Details	CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL

Chain	Residue	Details
A	ASN275-LEU282

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00504","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00504","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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