Structure of PDB 5t13 Chain A Binding Site BS02

Receptor Information

>5t13 Chain A (length=376) Species: 550 (Enterobacter cloacae)

HHHHHHMQAQVFRVPMSNPADVSGVAKLIDEGVIRAEEVVCVLGKTEGNG
CVNDFTRGYTTLAFKVYFSEKLGVSRQEVGERIAFIMSGGTEGVMAPHCT
IFTVQKTDNKQKTAAEGKRLAVQQIFTREFLPEEIGRMPQVTETADAVRR
AMREAGIADASDVHFVQVKCPLLTAGRMHDAVERGHTVATEDTYESMGYS
RGASALGIALALGEVEKANLSDEVITADYSLYSSVASTSAGIELMNNEII
VMGNSRAWGGDLVIGHAEMKDAIDGAAVRQALRDVGCCENDLPTVDELGR
VVNVFAKAEASPDGEVRNRRHTMLDDSDINSTRHARAVVNAVIASIVGDP
MVYVSGGSEHQGPAGGGPVAVIARTA

Ligand information

• Ligand ID: CO2
• InChI: InChI=1S/CO2/c2-1-3
• InChIKey: CURLTUGMZLYLDI-UHFFFAOYSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: C(=O)=O
  ACDLabs 10.04
  CACTVS 3.341: O=C=O
• Formula: C O2
• Name: CARBON DIOXIDE
• ChEMBL: CHEMBL1231871
• DrugBank: DB09157
• PDB chain: 5t13 Chain A Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5t13 Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel.
• Resolution: 2.19 Å
• Binding residue (original residue number in PDB): R51 G235 I236 E237
• Binding residue (residue number reindexed from 1): R57 G241 I242 E243
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.2.15: cyanuric acid amidohydrolase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
• GO:0018753 cyanuric acid amidohydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0019381 atrazine catabolic process

External links

• PDB: RCSB:5t13, PDBe:5t13, PDBj:5t13
• PDBsum: 5t13
• PubMed: 28345631
• UniProt: P0A3V4|CAH_ENTCL Cyanuric acid amidohydrolase (Gene Name=trzD)