MolNFT v1 · #144158 · protein
Novel modes of inhibition of wild-type IDH1: non-equivalent allosteric inhibition with CMPD3
6BKZ: “Novel modes of inhibition of wild-type IDH1: non-equivalent allosteric inhibition with CMPD3”. X-ray diffraction, 2 ligands (NAP, DWM). MolNFT v1 #144158 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BKZ
- Type
- protein
- Length
- 824 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O75874
- Ligands
- NAP, DWM
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 412 | — | O75874 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- DWM · (7R)-1-[(4-fluorophenyl)methyl]-N-{3-[(1R)-1-hydroxyethyl]phenyl}-7-methyl-5-(1H-pyrrole-2-carbonyl)-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-c]pyridine-3-carboxamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BKZ · Novel Modes of Inhibition of Wild-Type IDH1: Non-equivalent Allosteric Inhibition with… · the same entry in another collection · chain A against A, TM-score 1.00
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 O75874
- Elsewhere: RCSB PDB 6BKZ · PDBe 6BKZ · UniProt O75874
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