Structure of PDB 6muj Chain A Binding Site BS03

Receptor Information
>6muj Chain A (length=289) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARPRSTRGQVRLPGGEFAMGDAFGEGYPADGETPVHTVRLRPFHIDETAV
TNARFAAFVKATGHVTDAERFGSSAVFHLVVAAPDADVLGSAAGAPWWIN
VRGAHWRRPEGARSDITGRPNHPVVHVSWNDATAYARWAGKRLPTEAEWE
YAARGGLAGRRYAWGDELTPGGRWRCNIWQGRFPHVNTAEDGHLSTAPVK
SYRPNGHGLWNTAGNVWEWCSDWFSPTYYAESPTVDPHGPGTGAARVLRG
GSYLCHDSYCNRYRVAARSSNTPDSSSGNLGFRCANDAD
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain6muj Chain A Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6muj Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O2activation.
Resolution2.249 Å
Binding residue
(original residue number in PDB)
H95 H202
Binding residue
(residue number reindexed from 1)
H78 H185
Annotation score1
Enzymatic activity
Enzyme Commision number 1.8.3.7: formylglycine-generating enzyme.
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0120147 formylglycine-generating oxidase activity
GO:1903135 cupric ion binding
Biological Process
GO:0018158 protein oxidation
GO:0043687 post-translational protein modification

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Molecular Function

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Biological Process
External links
PDB RCSB:6muj, PDBe:6muj, PDBj:6muj
PDBsum6muj
PubMed30824597
UniProtQ9F3C7|FGE_STRCO Formylglycine-generating enzyme (Gene Name=SCO7548)

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