Structure of PDB 1oik Chain A

Receptor sequence
>1oikA (length=240) Species: 303 (Pseudomonas putida) [Search protein sequence]
LELDVHPVAGRIGAEIRGVKLSPDLDAATVEAIQAALVRHKVIFFRGQTH
LDDQSQEGFAKLLGEPVAHRANSWHTDVTFVEAYPKASILRSVVAPASGG
DTVWANTAAAYQELPEPLRELADKLWAVHSNRYETEHPVVRVHPISGERA
LQLGHFVKRIKGYSLADSQHLFAVLQGHVTRLENTVRWRWEAGDVAIWDN
RATQHYAVDDYGTQPRIVRRVTLAGEVPVGVDGQLSRTTR
3D structure
PDB1oik Crystal Structure of the Alkylsulfatase Atsk: Insights Into the Catalytic Mechanism of the Fe(II) Alpha-Ketoglutarate-Dependent Dioxygenase Superfamily
ChainA
Resolution2.06 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) H108 D110 H264 R279
Catalytic site (residue number reindexed from 1) H75 D77 H205 R220
Enzyme Commision number 1.14.11.77: alkyl sulfatase.
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 C26 A H81 A104 D110 V111 F215 H69 A71 D77 V78 F156
BS02 AKG A H108 D110 T135 H264 R275 R279 H75 D77 T102 H205 R216 R220
BS03 FE2 A H108 D110 H264 H75 D77 H205
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:1oik, PDBe:1oik, PDBj:1oik
PDBsum1oik
PubMed15023059
UniProtQ9WWU5|ATSK_PSEPU Alpha-ketoglutarate-dependent sulfate ester dioxygenase (Gene Name=atsK)

[Back to BioLiP]