Structure of PDB 3e2t Chain A

Receptor sequence
>3e2tA (length=307) Species: 9031 (Gallus gallus) [Search protein sequence]
NIPWYPKKISDLDKCANRVLMYGSDLDADHPGFKDNVYRKRRKYFADLAM
NYKHGDPIPEIEFTEEEIKTWGTVYRELNKLYPTHACREYLKNLPLLTKY
CGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCT
QYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASDE
AVQKLATCYFFTVEFGLCKQEGQLRVYGAGLLSSISELKHSLSGSAKVKP
FDPKVTCKQECLITTFQEVYFVSESFEEAKEKMREFAKTIKRPFGVKYNP
YTQSVQI
3D structure
PDB3e2t Crystal structure of tryptophan hydroxylase with bound amino acid substrate
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H273 H278 E318 S337
Catalytic site (residue number reindexed from 1) H169 H174 E214 S233
Enzyme Commision number 1.14.16.4: tryptophan 5-monooxygenase.
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 FE A H273 H278 E318 H169 H174 E214
BS02 IMD A H273 H278 E318 H169 H174 E214
BS03 TRP A R258 Y265 T266 E268 P269 H273 F319 S337 I367 R154 Y161 T162 E164 P165 H169 F215 S233 I263
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3e2t, PDBe:3e2t, PDBj:3e2t
PDBsum3e2t
PubMed18937498
UniProtP70080|TPH1_CHICK Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

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