Structure of PDB 1gqw Chain B

Receptor sequence

>1gqwB (length=273) Species: 562 (Escherichia coli)

ERLSITPLGPYIGAQISGADRPLSDNQFEQLYHAVLRHQVVFLRDQAITP
QQQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTF
IETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHD
FRKSFPEYKYEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFVNEGFTTR
IVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRVTQHYANA
DYLPQRRIMHRATILGDKPFYRA

3D structure

• PDB: 1gqw X-Ray Crystal Structure of Escherichia Coli Taurine/Alpha-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates
• Chain: B
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H99 D101 H255 R270
• Catalytic site (residue number reindexed from 1): H95 D97 H246 R261
• 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	B	H99 D101 H255	H95 D97 H246
BS02	AKG	B	N95 H99 D101 H255 A257 R266 R270	N91 H95 D97 H246 A248 R257 R261

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

External links

• PDB: RCSB:1gqw, PDBe:1gqw, PDBj:1gqw
• PDBsum: 1gqw
• PubMed: 11955067
• UniProt: P37610|TAUD_ECOLI Alpha-ketoglutarate-dependent taurine dioxygenase (Gene Name=tauD)