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Crystal structure of human indoleamine 2,3-dioxygenase 1 (IDO1) in complex with a bms-978587 analog
Analyse Crystal structure of human indoleamine 2,3-dioxygenase 1 (IDO1) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E43
- Type
- protein
- Length
- 1,495 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14902
- Ligands
- HQM, BEZ
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 372 | — | P14902 |
| B | — | protein | 373 | — | P14902 |
| C, D | — | protein | 375 | — | P14902 |
Ligands and binding sites
- HQM · (1R,2S)-2-(4-[cyclohexyl(2-methylpropyl)amino]-3-{[(4-methylphenyl)carbamoyl]amino}phenyl)cyclopropane-1-carboxylic acid · ligand · 4 copies · chains A, B, C, D
- BEZ · Benzoic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6E43 · Crystal structure of human indoleamine 2,3-dioxygenase 1 (IDO1) in complex with a… · the same entry in another collection · chain A against A, TM-score 1.00
- P14902 · AlphaFold monomer V2.0 prediction for indoleamine 2,3-dioxygenase 1 (P14902) · a predicted model of the same protein · chain B 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 P14902
- Elsewhere: RCSB PDB 6E43 · PDBe 6E43 · UniProt P14902
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