Structure of PDB 1bll Chain E Binding Site BS02

Receptor Information
>1bll Chain E (length=481) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TKGLVLGIYSKEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRT
FYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDL
EIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEA
WQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIR
PKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGIT
FDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLAPLC
ENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKV
IINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLF
EHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGV
MTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQ
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1bll Chain E Residue 488 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bll X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D255 D332 E334
Binding residue
(residue number reindexed from 1)		D252 D329 E331
Annotation score1
Enzymatic activity
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
3.4.11.5: prolyl aminopeptidase.
3.4.13.23: cysteinylglycine-S-conjugate dipeptidase.
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004180 carboxypeptidase activity
GO:0008233 peptidase activity
GO:0016805 dipeptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
GO:0097718 disordered domain specific binding
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bll, PDBe:1bll, PDBj:1bll
PDBsum1bll
PubMed8357796
UniProtP00727|AMPL_BOVIN Cytosol aminopeptidase (Gene Name=LAP3)

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