Research workbench
Crystal structure of K-RAS(G12D) gppnhp bound to cyclic peptide ligand KD2
Analyse Crystal structure of K-RAS(G12D) gppnhp bound to cyclic peptide ligand KD2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WGN
- Type
- protein
- Length
- 536 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01116
- Ligands
- GNP, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 166 | — | P01116 |
| B | — | protein | 162 | — | P01116 |
| C | — | protein | 163 | — | P01116 |
| E, F, G | — | protein | 15 | — | — |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WGN · Crystal structure of K-Ras(G12D) GppNHp bound to cyclic peptide ligand KD2 · 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 P01116
- Elsewhere: RCSB PDB 6WGN · PDBe 6WGN · UniProt P01116
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