Structure of PDB 2nwb Chain A

Receptor sequence
>2nwbA (length=379) Species: 211586 (Shewanella oneidensis MR-1) [Search protein sequence]
TYNTEAFDEWIRSRFVELNSQLEQLYYQQTDRANVQEVGTELKHTLESEG
RELVKALLDEGNTDEGFDSAFDLLGNVGLYMAACRRHEITEPTRETTSPL
LEASALAMHIGASIGVTPRFATAHLTTHNRAHNGIYKRFTDLPDEKLFVD
YNTKGILAYKRASDALLKIQPLGISHPISHDLLRVTKQALQDVIESNQQL
FNRLDTDRFFYCVRPYYKPYRVGSVVYRGANAGDFAGINVIDLTLGLCFA
NEASYSQMLVDKFLYMMPEDQQILRECMRRPNLMDDFLQAKGCIHQDWYQ
ENLKLFIEVCELHGQTAIQHHNELVTKYIAEPSVSMPLHVLLASLERLRD
RRAAVLRDDIRTRYYDLKKLKDSLRLEHH
3D structure
PDB2nwb Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.11: tryptophan 2,3-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 HEM A F152 N156 Y163 N235 A236 G237 I242 H324 Y332 I333 L365 R369 F148 N152 Y159 N231 A232 G233 I238 H320 Y328 I329 L348 R352
Gene Ontology
Molecular Function
GO:0003674 molecular_function
GO:0004833 tryptophan 2,3-dioxygenase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
GO:0019441 tryptophan catabolic process to kynurenine

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Molecular Function
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Biological Process
External links
PDB RCSB:2nwb, PDBe:2nwb, PDBj:2nwb
PDBsum2nwb
PubMed17197414
UniProtQ8E972

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