Structure of PDB 6edh Chain B

Receptor sequence

>6edhB (length=281) Species: 83333 (Escherichia coli K-12)

ERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAI
TPQQQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDV
TFIETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAE
HDFRKSFPEYKYRKTEEEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFV
NEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRV
TQHYANADYLPQRRIMHRATILGDKPFYRAG

3D structure

• PDB: 6edh Structure of a Ferryl Mimic in the Archetypal Iron(II)- and 2-(Oxo)-glutarate-Dependent Dioxygenase, TauD.
• Chain: B
• Resolution: 1.73 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H99 D101 H255 R270
• Catalytic site (residue number reindexed from 1): H97 D99 H253 R268
• 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	VVO	B	N95 H99 D101 H255 R270	N93 H97 D99 H253 R268

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:6edh, PDBe:6edh, PDBj:6edh
• PDBsum: 6edh
• PubMed: 31503454
• UniProt: P37610|TAUD_ECOLI Alpha-ketoglutarate-dependent taurine dioxygenase (Gene Name=tauD)