Research workbench
Crystal structure of KRAS4A(GMPPNP-bound) in complex with the RAS- binding DOMAIN(RBD) of SIN1
Analyse Crystal structure of KRAS4A(GMPPNP-bound) in complex with the RAS- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VVB
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Target of rapamycin complex 2 subunit MAPKAP1; GTPase KRAS
- EC
- 3.6.5.2
- UniProt
- Q9BPZ7, P01116
- Ligands
- GNP, MG
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Target of rapamycin complex 2 subunit MAPKAP1 | protein | 77 | 22% helix, 32% strand | Q9BPZ7 |
| A | GTPase KRAS (EC 3.6.5.2) | protein | 167 | 39% helix, 26% strand | P01116 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.67 | 0.82 | 45 | MG, GNP |
Interfaces
1 interface between chains.
- B–A · 595 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7VVB · Crystal Structure of KRas4A(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of… · the same entry in another collection · chain B against B, TM-score 1.00
- Q9BPZ7 · AlphaFold monomer V2.0 prediction for target of rapamycin complex 2 subunit MAPKAP1… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q9BPZ7
- Every structure of UniProt P01116
- Elsewhere: RCSB PDB 7VVB · PDBe 7VVB · UniProt Q9BPZ7 · UniProt P01116
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