Structure of PDB 3gts Chain A

Receptor sequence
>3gtsA (length=341) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
ATFVRNAWYVAALPEELSEKPLGRTILDTPLALYRQPDGVVAALLDICPH
RFAPLSDGILVNGHLQCPYHGLEFDGGGQCVHNPHGNGARPASLNVRSFP
VVERDALIWIWPGDPALADPGAIPDFGCRVDPAYRTVGGYGHVDCNYKLL
VDNLMDLGHAQYVHRANAQTDAFDRLEREVIVGDGEIQALMKIPGGTPSV
LMAKFLRGANTPVDAWNDIRWNKVSAMLNFIAVAPEGTPKEQSIHSRGTH
ILTPETEASCHYFFGSSRNFGIDDPEMDGVLRSWQAQALVKEDKVVVEAI
ERRRAYVEANGIRPAMLSCDEAAVRVSREIEKLEQLEAARL
3D structure
PDB3gts Dicamba monooxygenase: structural insights into a dynamic Rieske oxygenase that catalyzes an exocyclic monooxygenation.
ChainA
Resolution2.2 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 1.14.15.-
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 FES A C49 H51 R52 C68 Y70 H71 L73 C48 H50 R51 C67 Y69 H70 L72
BS02 FE A H160 H165 D294 H159 H164 D293
BS03 D3M A N230 H251 W285 N229 H250 W284
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0046872 metal ion binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3gts, PDBe:3gts, PDBj:3gts
PDBsum3gts
PubMed19616009
UniProtQ5S3I3|DDMC_STEMA Dicamba O-demethylase, oxygenase component (Gene Name=ddmC)

[Back to BioLiP]