Structure of PDB 5ypj Chain A Binding Site BS02

Receptor Information
>5ypj Chain A (length=282) Species: 419947 (Mycobacterium tuberculosis H37Ra) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVA
GRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKS
CNTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVA
DEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFT
GHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDD
GWTVVTKDRKWTAQFEHTLLVTDTGVEILTAL
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain5ypj Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ypj Discovery of a new class of type 1 methionine aminopeptidases that have relaxed substrate specificity.
Resolution2.01 Å
Binding residue
(original residue number in PDB)
D131 D142 E269
Binding residue
(residue number reindexed from 1)
D128 D139 E266
Annotation score3
Enzymatic activity
Enzyme Commision number 3.4.11.18: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5ypj, PDBe:5ypj, PDBj:5ypj
PDBsum5ypj
PubMed30763644
UniProtA5U6L5

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