Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3H8F

High pH native structure of leucine aminopeptidase from Pseudomonas putida

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0016787	molecular_function	hydrolase activity
A	0019538	biological_process	protein metabolic process
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008235	molecular_function	metalloexopeptidase activity
B	0016787	molecular_function	hydrolase activity
B	0019538	biological_process	protein metabolic process
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity
C	0004177	molecular_function	aminopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008235	molecular_function	metalloexopeptidase activity
C	0016787	molecular_function	hydrolase activity
C	0019538	biological_process	protein metabolic process
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
D	0004177	molecular_function	aminopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008235	molecular_function	metalloexopeptidase activity
D	0016787	molecular_function	hydrolase activity
D	0019538	biological_process	protein metabolic process
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0070006	molecular_function	metalloaminopeptidase activity
E	0004177	molecular_function	aminopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008235	molecular_function	metalloexopeptidase activity
E	0016787	molecular_function	hydrolase activity
E	0019538	biological_process	protein metabolic process
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0070006	molecular_function	metalloaminopeptidase activity
F	0004177	molecular_function	aminopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0008235	molecular_function	metalloexopeptidase activity
F	0016787	molecular_function	hydrolase activity
F	0019538	biological_process	protein metabolic process
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	LYS267
A	ASP272
A	ASP290
A	GLU351
A	MN502
A	BCT504
A	HOH3681

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 502

Chain	Residue
A	GLU351
A	ZN501
A	HOH3681
A	ASP272
A	ASP349

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 503

Chain	Residue
A	LEU189
A	GLY190
A	LEU192
A	LYS288
A	MET291
A	HOH520

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT A 504

Chain	Residue
A	LYS267
A	ALA350
A	GLU351
A	GLY352
A	ARG353
A	LEU377
A	ZN501
A	HOH3681

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 501

Chain	Residue
B	LYS267
B	ASP272
B	ASP290
B	GLU351
B	MN502
B	BCT504
B	HOH3682

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 502

Chain	Residue
B	ASP272
B	ASP349
B	GLU351
B	ZN501
B	HOH3682

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 503

Chain	Residue
B	LEU189
B	GLY190
B	LEU192
B	LYS288
B	MET291
B	HOH3687

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT B 504

Chain	Residue
B	LYS267
B	ALA350
B	GLU351
B	GLY352
B	ARG353
B	LEU377
B	ZN501
B	HOH3682

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN C 501

Chain	Residue
C	LYS267
C	ASP272
C	ASP290
C	GLU351
C	MN502
C	BCT504
C	HOH3683

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 502

Chain	Residue
C	ASP272
C	ASP349
C	GLU351
C	ZN501
C	HOH3683

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 503

Chain	Residue
C	LEU189
C	GLY190
C	LEU192
C	LYS288
C	MET291
C	HOH2007

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT C 504

Chain	Residue
C	LYS267
C	ALA350
C	GLU351
C	GLY352
C	ARG353
C	LEU377
C	ZN501
C	HOH3683

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN D 501

Chain	Residue
D	LYS267
D	ASP272
D	ASP290
D	GLU351
D	MN502
D	BCT504
D	HOH3684

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 502

Chain	Residue
D	ASP272
D	ASP349
D	GLU351
D	ZN501
D	HOH3684

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 503

Chain	Residue
D	LEU189
D	GLY190
D	LEU192
D	LYS288
D	MET291
D	HOH511

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT D 504

Chain	Residue
D	GLU351
D	GLY352
D	ARG353
D	LEU377
D	ZN501
D	HOH3684
D	LYS267
D	ASP349
D	ALA350

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN E 501

Chain	Residue
E	LYS267
E	ASP272
E	ASP290
E	GLU351
E	MN502
E	BCT504
E	HOH3685

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 502

Chain	Residue
E	ASP272
E	ASP349
E	GLU351
E	ZN501
E	HOH3685

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 503

Chain	Residue
E	LEU189
E	GLY190
E	LEU192
E	LYS288
E	MET291
E	HOH556

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT E 504

Chain	Residue
E	LYS267
E	ALA350
E	GLU351
E	GLY352
E	ARG353
E	LEU377
E	ZN501
E	HOH3685

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN F 501

Chain	Residue
F	LYS267
F	ASP272
F	ASP290
F	GLU351
F	MN502
F	HOH3686

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 502

Chain	Residue
F	ASP272
F	ASP349
F	GLU351
F	ZN501
F	HOH3686

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K F 503

Chain	Residue
F	LEU189
F	GLY190
F	LEU192
F	LYS288
F	MET291
F	HOH508

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCT F 504

Chain	Residue
F	LYS267
F	ALA350
F	GLU351
F	GLY352
F	ARG353
F	LEU377
F	HOH3686

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN347-LEU354

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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