Structure of PDB 3n9t Chain A Binding Site BS01

Receptor Information

>3n9t Chain A (length=286) Species: 303 (Pseudomonas putida)

YKAVEALISDQAVDSFETSPNPRFKQIMQSLVRHLHDFVSEVELTEQEWF
EGIRFLTATGQKCDGKVRQEFILLSDTLGVSMLVDAINHRQSTNATETTV
FGPFFIEGMPDRGYGENMALTDGVPALVYGRVLDVQGRPVVGAVLDVWQT
ADNGMYSGQDPDQPFGNLRGRYRSDNDGCFAIQTTVPVCYPIPTDGPVGE
MLDAANRHAWRPAHLHFMIQAPGYRKLVTHLFNSDDPYLDSDAVFGVKGS
LQVKYEDRPAHDEDAGGLDMPYPYKSAYYEFVMEAE

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: 3n9t Chain A Residue 292

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3n9t Cryatal structure of Hydroxyquinol 1,2-dioxygenase from Pseudomonas putida DLL-E4
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): Y160 Y194 H218 H220
• Binding residue (residue number reindexed from 1): Y156 Y190 H214 H216
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y160 Y194 R215 H218 H220
• Catalytic site (residue number reindexed from 1): Y156 Y190 R211 H214 H216
• Enzyme Commision number: 1.13.11.37: hydroxyquinol 1,2-dioxygenase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005506 iron ion binding
• GO:0008199 ferric iron binding
• GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
• GO:0018576 catechol 1,2-dioxygenase activity
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

Biological Process

• GO:0009712 catechol-containing compound metabolic process

External links

• PDB: RCSB:3n9t, PDBe:3n9t, PDBj:3n9t
• PDBsum: 3n9t
• UniProt: C6FI44