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Structure of PDB 1bpm Chain A Binding Site BS01

Receptor Information
>1bpm Chain A (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 IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1bpm Chain A Residue 488 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1bpm Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.
Resolution2.9 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
Catalytic site (original residue number in PDB) K262 R336
Catalytic site (residue number reindexed from 1) K259 R333
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:1bpm, PDBe:1bpm, PDBj:1bpm
PDBsum1bpm
PubMed8506345
UniProtP00727|AMPL_BOVIN Cytosol aminopeptidase (Gene Name=LAP3)

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