Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3H8G

Bestatin complex 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	BES505

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

Chain	Residue
A	GLU351
A	ZN501
A	BES505
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	HOH514

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	BES505

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE BES A 505

Chain	Residue
A	LYS267
A	ASP272
A	LYS279
A	MET287
A	ASP290
A	ASP349
A	GLU351
A	THR376
A	LEU377
A	THR378
A	GLY379
A	ILE437
A	ALA466
A	TRP470
A	ZN501
A	MN502
A	BCT504
A	HOH2935
A	HOH2940

site_id	AC6
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	BES505

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 502

Chain	Residue
B	ASP272
B	ASP349
B	GLU351
B	ZN501
B	BES505

site_id	AC8
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	HOH524

site_id	AC9
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	BES505

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BES B 505

Chain	Residue
B	LYS267
B	ASP272
B	LYS279
B	MET287
B	ASP290
B	ASP349
B	GLU351
B	THR376
B	LEU377
B	THR378
B	GLY379
B	ALA466
B	TRP470
B	ZN501
B	MN502
B	BCT504
B	HOH2809
B	HOH3487

site_id	BC2
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	BES505

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 502

Chain	Residue
C	ZN501
C	BES505
C	ASP272
C	ASP349
C	GLU351

site_id	BC4
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	HOH518

site_id	BC5
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	BES505

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BES C 505

Chain	Residue
C	LYS267
C	ASP272
C	LYS279
C	MET287
C	ASP290
C	ASP349
C	GLU351
C	THR376
C	LEU377
C	THR378
C	GLY379
C	ALA466
C	TRP470
C	ZN501
C	MN502
C	BCT504
C	HOH2928
C	HOH3103

site_id	BC7
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	BES505

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 502

Chain	Residue
D	ASP272
D	ASP349
D	GLU351
D	ZN501
D	BES505

site_id	BC9
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	HOH526

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT D 504

Chain	Residue
D	LYS267
D	ALA350
D	GLU351
D	GLY352
D	ARG353
D	LEU377
D	ZN501
D	BES505

site_id	CC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BES D 505

Chain	Residue
D	LYS267
D	ASP272
D	LYS279
D	MET287
D	ASP290
D	ASP349
D	GLU351
D	THR376
D	LEU377
D	THR378
D	GLY379
D	TRP470
D	ZN501
D	MN502
D	BCT504
D	HOH819
D	HOH3344

site_id	CC3
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	BES505

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

Chain	Residue
E	ASP272
E	ASP349
E	GLU351
E	ZN501
E	BES505

site_id	CC5
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	HOH510

site_id	CC6
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	BES505

site_id	CC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BES E 505

Chain	Residue
E	LYS267
E	ASP272
E	LYS279
E	MET287
E	ASP290
E	ASP349
E	GLU351
E	THR376
E	LEU377
E	THR378
E	GLY379
E	ALA466
E	TRP470
E	ZN501
E	MN502
E	BCT504
E	HOH1267
E	HOH2741

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN F 501

Chain	Residue
F	LYS267
F	ASP272
F	ASP290
F	GLU351
F	MN502
F	BCT504
F	BES505

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 502

Chain	Residue
F	ASP272
F	ASP349
F	GLU351
F	ZN501
F	BES505

site_id	DC1
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	HOH518

site_id	DC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT F 504

Chain	Residue
F	LYS267
F	ALA350
F	GLU351
F	GLY352
F	ARG353
F	LEU377
F	ZN501
F	BES505

site_id	DC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BES F 505

Chain	Residue
F	LYS267
F	ASP272
F	LYS279
F	MET287
F	ASP290
F	ASP349
F	GLU351
F	THR376
F	LEU377
F	THR378
F	GLY379
F	ALA466
F	TRP470
F	ZN501
F	MN502
F	BCT504
F	HOH1648

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
F	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)