Structure of PDB 8aq0 Chain A Binding Site BS04

Receptor Information

>8aq0 Chain A (length=410) Species: 382 (Sinorhizobium meliloti)

ENRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEE
AGLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLS
GLEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEY
AYARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAEN
KQIGVVTHCQGGWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQT
VAMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRAR
IEAEAPKICERLGVGCSIEAVGHCDPVTFDPKLVETVRGAAEKLGYSHMN
LVSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLF
HAVLETAEIV

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 8aq0 Chain A Residue 504

Receptor-Ligand Complex Structure

Structure summary

• PDB: 8aq0 Selecting Better Biocatalysts by Complementing Recoded Bacteria.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): D98 E133 H386
• Binding residue (residue number reindexed from 1): D93 E128 H381
• Annotation score: 1

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

External links

• PDB: RCSB:8aq0, PDBe:8aq0, PDBj:8aq0
• PDBsum: 8aq0
• PubMed: 36342942
• UniProt: Q6DTN4|HYUC_RHIML N-carbamoyl-L-amino-acid hydrolase (Gene Name=hyuC)