MolNFT v1 · #129178 · protein
Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.
5OCO: “Discovery of small molecules binding to KRAS via high affinity antibody fragment competition method.”. X-ray diffraction, 3 ligands (GNP, 9RK, MG). MolNFT v1 #129178 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OCO
- Type
- protein
- Length
- 1,034 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01116
- Ligands
- GNP, 9RK, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, E | — | protein | 173 | — | P01116 |
| A, C, D, F | — | protein | 172 | — | P01116 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 6 copies · chains B, A, C, D, E, F
- 9RK · ~{N}-[[(3~{R})-2,3-dihydro-1,4-benzodioxin-3-yl]methyl]furan-2-carboxamide · ligand · 5 copies · chains B, C, D, E, F
- MG · Magnesium ion · metal · 6 copies · chains B, A, C, D, E, F
- CIT · Citric acid · additive · 3 copies · chains A, D
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P01116
- Elsewhere: RCSB PDB 5OCO · PDBe 5OCO · UniProt P01116
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