Structure of PDB 1gqw Chain A

Receptor sequence
>1gqwA (length=277) Species: 562 (Escherichia coli) [Search protein sequence]
RLSITPLGPYIGAQISGADRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQ
QQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFI
ETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDF
RKSFPEYKYRKTEEEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFVNEG
FTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRVTQH
YANADYLPQRRIMHRATILGDKPFYRA
3D structure
PDB1gqw X-Ray Crystal Structure of Escherichia Coli Taurine/Alpha-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H99 D101 H255 R270
Catalytic site (residue number reindexed from 1) H94 D96 H250 R265
Enzyme Commision number 1.14.11.17: taurine 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 FE2 A H99 D101 H255 H94 D96 H250
BS02 AKG A N95 H99 D101 L114 T126 W240 H255 A257 R266 M268 R270 N90 H94 D96 L109 T121 W235 H250 A252 R261 M263 R265
Gene Ontology
Molecular Function
GO:0000908 taurine dioxygenase activity
GO:0008198 ferrous iron binding
GO:0016491 oxidoreductase activity
GO:0031418 L-ascorbic acid binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006790 sulfur compound metabolic process
GO:0019529 taurine catabolic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:1990205 taurine dioxygenase complex

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External links
PDB RCSB:1gqw, PDBe:1gqw, PDBj:1gqw
PDBsum1gqw
PubMed11955067
UniProtP37610|TAUD_ECOLI Alpha-ketoglutarate-dependent taurine dioxygenase (Gene Name=tauD)

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