Structure of PDB 2gbx Chain A

Receptor sequence
>2gbxA (length=449) Species: 13690 (Sphingobium yanoikuyae) [Search protein sequence]
TLVDTVNASQSRQVFWDEDVYALEIERIFSRAWLMLGHESLVPKPGDFIT
TYMAEDKVILSHQSDGTFRAFINSCSHRGNQICHADSGNAKAFVCNYHGW
VFGQDGSLVDVPLESRCYHNSLDKQKLAAKSVRVETYKGFIFGCHDPEAP
SLEDYLGEFRYYLDTIWEGAGGGMELLGPPMKSLLQCNWKVPAENFIGDG
YHVGWTHAAALSQIGGELAGLAGNRADIPFDDLGLQFTTRHGHGFGVIDN
AAAGLHIKREGWTKFLEDTRGEVRRKFGPERERLYLGHWNCSIFPNCSFL
YGTNTFKIWHPRGPHEIEVWTYTIVPRDADPATKSMIQREAIRTFGTAGT
LESDDGENMSSATYINRGVITRNGRMNSTMGVGYEGPHPVYPGIVGISFI
GETSYRGFYRFWKEMIDAPDWASVKANDDTWDSVFPNRNFWNEKLNAAE
3D structure
PDB2gbx Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H103 D204 H207 H212 D360
Catalytic site (residue number reindexed from 1) H98 D199 H202 H207 D355
Enzyme Commision number ?
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 H207 H212 D360 H202 H207 D355
BS02 FES A C80 H82 R83 C100 Y102 H103 W105 C75 H77 R78 C95 Y97 H98 W100
BS03 BNL A D204 V208 L260 H293 N295 L305 D199 V203 L255 H288 N290 L300
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0044237 cellular metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2gbx, PDBe:2gbx, PDBj:2gbx
PDBsum2gbx
PubMed17349044
UniProtA2TC87

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