Structure of PDB 1lcp Chain A Binding Site BS01

Receptor Information
>1lcp Chain A (length=484) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGK
TRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQI
QDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSED
QEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDV
FIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGK
GITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLA
PLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFN
PKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRM
PLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDI
AGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQ
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 chain1lcp Chain A Residue 488 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lcp Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form.
Resolution1.65 Å
Binding residue
(original residue number in PDB)		D255 D332 E334
Binding residue
(residue number reindexed from 1)		D255 D332 E334
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K262 R336
Catalytic site (residue number reindexed from 1) K262 R336
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:1lcp, PDBe:1lcp, PDBj:1lcp
PDBsum1lcp
PubMed7619821
UniProtP00727|AMPL_BOVIN Cytosol aminopeptidase (Gene Name=LAP3)

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