Research workbench
Crystal structure of human tdo in complex with TRP and dioxygen, northeast structural genomics consortium target HR6161
Analyse Crystal structure of human tdo in complex with TRP and dioxygen, northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TI9
- Type
- protein
- Length
- 1,352 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48775
- Ligands
- HEM, OXY, PO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 352 | — | P48775 |
| B | — | protein | 338 | — | P48775 |
| C | — | protein | 328 | — | P48775 |
| D | — | protein | 334 | — | P48775 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- OXY · Oxygen molecule · ion · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P48775 · AlphaFold monomer V2.0 prediction for tryptophan 2,3-dioxygenase (P48775) · a predicted model of the same protein · chain C against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P48775
- Elsewhere: RCSB PDB 5TI9 · PDBe 5TI9 · UniProt P48775
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