Structure of PDB 3wku Chain A

Receptor sequence
>3wkuA (length=407) Species: 627192 (Sphingobium sp. SYK-6) [Search protein sequence]
AKIIGGFAVSHTPTIAFAHDDPVWAPIFQGFEPVKQWLAEQKPDVTFYVY
NDHMTSFFEHYSHFALGVGEEYSPADEGGGQRDLPPIKGDPELAKHIAEC
LVADEFDLAYWQGMGLDHGAFSPLSVLLPHEHGWPCRIVPLQCGVLQHPI
PKARRFWNFGRSLRRAIQSYPRDIKVAIAGTGGLSHQVHGERAGFNNTEW
DMEFMERLANDPESLLGATVTDLAKKGGWEGAEVVMWLLMRGALSPEVKT
LHQSYFLPSMTAIATMLFEDQGDAAPPAESDEALRARAKRELAGVEEIEG
TYPFTIDRAVKGFRINHFLHRLIEPDFRKRFVEDPEGLFAESDLTEEEKS
LIRNRDWIGMIHYGVIFFMLEKMAAVLGIGNIDVYAAFRGLSVPEFQKTR
NAAITYS
3D structure
PDB3wku Molecular Mechanism of Strict Substrate Specificity of an Extradiol Dioxygenase, DesB, Derived from Sphingobium sp. SYK-6
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H12 H59 H192 E239
Catalytic site (residue number reindexed from 1) H11 H53 H186 E233
Enzyme Commision number 1.13.11.58: linoleate 9S-lipoxygenase.
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 H12 N57 H59 E239 H11 N51 H53 E233
BS02 GDE A F374 E377 Y391 Y412 F368 E371 Y385 Y406
Gene Ontology
Molecular Function
GO:0008198 ferrous iron binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:3wku, PDBe:3wku, PDBj:3wku
PDBsum3wku
PubMed24657997
UniProtG2IKE5

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