Structure of PDB 8apz Chain B Binding Site BS05

Receptor Information
>8apz Chain B (length=410) Species: 382 (Sinorhizobium meliloti) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEEA
GLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLSG
LEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEYA
YARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAENK
QIGVVTHCQGLWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQTV
AMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRARI
EAEAPKICERLGVGCSIEAVGHFDPVTFDPKLVETVRGAAEKLGYSHMNL
VSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLFH
AVLETAEIVE
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain8apz Chain B Residue 504 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8apz Selecting Better Biocatalysts by Complementing Recoded Bacteria.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		D98 E133 H386
Binding residue
(residue number reindexed from 1)		D92 E127 H380
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.87: N-carbamoyl-L-amino-acid hydrolase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
GO:0050538 N-carbamoyl-L-amino-acid hydrolase activity
Biological Process
GO:0008652 amino acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8apz, PDBe:8apz, PDBj:8apz
PDBsum8apz
PubMed36342942
UniProtQ6DTN4|HYUC_RHIML N-carbamoyl-L-amino-acid hydrolase (Gene Name=hyuC)

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