Structure of PDB 8uw6 Chain D Binding Site BS03

Receptor Information
>8uw6 Chain D (length=381) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEV
QPVPGTRNKFNMLASTGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHD
GKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGAR
YFAETTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARG
VNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGDASNR
ICAWCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPI
PGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSIN
QAHQPDEYLETRFIKPTRELITQVIHHFCWH
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 chain8uw6 Chain D Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8uw6 Acetylornithine deacetylase from Escherichia coli, di-zinc form.
Resolution1.8 Å
Binding residue
(original residue number in PDB)
H378 H383
Binding residue
(residue number reindexed from 1)
H376 H381
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.16: acetylornithine deacetylase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008777 acetylornithine deacetylase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050897 cobalt ion binding
Biological Process
GO:0006526 L-arginine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8uw6, PDBe:8uw6, PDBj:8uw6
PDBsum8uw6
PubMed39055043
UniProtP23908|ARGE_ECOLI Acetylornithine deacetylase (Gene Name=argE)

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