Structure of PDB 3hjq Chain A

Receptor sequence

>3hjqA (length=256) Species: 37919 (Rhodococcus opacus)

ATADTSPERLAAIAKDALGALNDVILKHGVTYPEYRVFKQWLIDVGEGGE
WPLFLDVFIEHSVEEVLARSRKGTMGSIEGPYYIENSPELPSKCTLPMRE
EDEKITPLVFSGQVTDLDGNGLAGAKVELWHADNDGYYSQFAPHLPEWNL
RGTIIADEEGRYEITTIQPAPYQIPTDGPTGQFIEAQNGHPWRPAHLHLI
VSAPGKESVTTQLYFKGGEWIDSDVASATKPELILDPKTGDDGKNYVTYN
FVLDPA

3D structure

• PDB: 3hjq Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y162 Y196 R217 H220 H222
• Catalytic site (residue number reindexed from 1): Y138 Y172 R193 H196 H198
• 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	Y162 H220 H222	Y138 H196 H198
BS02	MBD	A	V81 I102 P105 Y106 Y162 R217 H220 H222	V57 I78 P81 Y82 Y138 R193 H196 H198	MOAD: Ki=6.5uM

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:0009056 catabolic process
• GO:0009712 catechol-containing compound metabolic process

External links

• PDB: RCSB:3hjq, PDBe:3hjq, PDBj:3hjq
• PDBsum: 3hjq
• PubMed: 20040374
• UniProt: P95607|CATA_RHOOP Catechol 1,2-dioxygenase (Fragment) (Gene Name=catA)