Structure of PDB 3o32 Chain B

Receptor sequence
>3o32B (length=255) Species: 37919 (Rhodococcus opacus) [Search protein sequence]
NTRVIELFDEFTDLIRDFIVRHEITTPEYETIMQYMISVGEAGEWPLWLD
AFFETTVDSVSYGKGNWTSSAIQGPFFKEGAPLLTGKPATLPMRADEPGD
RMRFTGSVRDTSGTPITGAVIDVWHSTNDGNYSFFSPALPDQYLLRGRVV
PAEDGSIEFHSIRPVPYEIPKAGPTGQLMNSYLGRHSWRPAHIHIRITAD
GYRPLITQLYFEGDPYLDSDSCSAVKSELVLPVNKIDIDGETWQLVDFNF
ILQHN
3D structure
PDB3o32 X-ray structures of 4-chlorocatechol 1,2-dioxygenase adducts with substituted catechols: new perspectives in the molecular basis of intradiol ring cleaving dioxygenases specificity.
ChainB
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y134 Y169 R191 H194 H196
Catalytic site (residue number reindexed from 1) Y132 Y167 R189 H192 H194
Enzyme Commision number 1.13.11.-
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 B H194 H196 H192 H194
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3o32, PDBe:3o32, PDBj:3o32
PDBsum3o32
PubMed23261399
UniProtO67987|CLCA_RHOOP Chlorocatechol 1,2-dioxygenase (Gene Name=clcA)

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