Structure of PDB 8apz Chain B Binding Site BS03

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 502 [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)		H87 D98 G99 E132 H194
Binding residue
(residue number reindexed from 1)		H81 D92 G93 E126 H188
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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