Structure of PDB 5vxt Chain A

Receptor sequence

>5vxtA (length=311) Species: 398577 (Burkholderia ambifaria MC40-6)

HHHHMSVKVFDTKEVQDLLKAASNAGAGNARTQQIVHRLLGDLFKAIDDL
DITPDEVWAGVNYLNKLGQDGEAALLAAGLGLEKYLDIRMDAEDEAIGLD
GGTPRTIEGPLYVAGAPVRDGVAKIDLDADEGAGPLVIHGTVTGLDGKPV
AGALVECWHANSHGFYSHFDPTGKQSDFNLRGAVKTGADGKYEFRTLMPV
GYGCPPQGATQQLLDRLGRHGNRPAHVHFFVTSDGHRKLTTQFNIEGDPL
IWDDFAYATREELIPPVTAKAGGAALGLKADAYQDIEFNFVLTPRVEGKD
NQIVERLRASA

3D structure

• PDB: 5vxt Crystal structure of catechol 1,2-dioxygenase from Burkholderia ambifaria
• Chain: A
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y170 Y206 R227 H230 H232
• Catalytic site (residue number reindexed from 1): Y166 Y202 R223 H226 H228
• Enzyme Commision number: 1.13.11.1: catechol 1,2-dioxygenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FE	A	Y170 H230 H232	Y166 H226 H228
BS02	CAQ	A	P114 Y170 Y206 R227 H232	P110 Y166 Y202 R223 H228

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
• GO:0019614 catechol-containing compound catabolic process
• GO:0042952 beta-ketoadipate pathway

External links

• PDB: RCSB:5vxt, PDBe:5vxt, PDBj:5vxt
• PDBsum: 5vxt
• UniProt: B1Z4S0