Structure of PDB 3n9t Chain A

Receptor sequence
>3n9tA (length=286) Species: 303 (Pseudomonas putida) [Search protein sequence]
YKAVEALISDQAVDSFETSPNPRFKQIMQSLVRHLHDFVSEVELTEQEWF
EGIRFLTATGQKCDGKVRQEFILLSDTLGVSMLVDAINHRQSTNATETTV
FGPFFIEGMPDRGYGENMALTDGVPALVYGRVLDVQGRPVVGAVLDVWQT
ADNGMYSGQDPDQPFGNLRGRYRSDNDGCFAIQTTVPVCYPIPTDGPVGE
MLDAANRHAWRPAHLHFMIQAPGYRKLVTHLFNSDDPYLDSDAVFGVKGS
LQVKYEDRPAHDEDAGGLDMPYPYKSAYYEFVMEAE
3D structure
PDB3n9t Cryatal structure of Hydroxyquinol 1,2-dioxygenase from Pseudomonas putida DLL-E4
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 Y160 Y194 H218 H220 Y156 Y190 H214 H216
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3n9t, PDBe:3n9t, PDBj:3n9t
PDBsum3n9t
PubMed
UniProtC6FI44

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