MolNFT v1 · #189768 · protein
Crystal structure of HRAS(GMPPNP-bound) in complex with the RAS- binding DOMAIN(RBD) of SIN1
7VV9 · GTPase HRAS: “Crystal structure of HRAS(GMPPNP-bound) in complex with the RAS- binding DOMAIN(RBD) of SIN1”. X-ray diffraction, 2 ligands (GNP, MG), 2 pockets (best druggability 0.67). MolNFT v1 #189768 on GenesisL1: 3D structure…
- PDB
- 7VV9
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase HRAS; Target of rapamycin complex 2 subunit MAPKAP1
- EC
- 3.6.5.2
- UniProt
- P01112, Q9BPZ7
- Ligands
- GNP, MG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase HRAS (EC 3.6.5.2) | protein | 166 | 39% helix, 27% strand | P01112 |
| C | Target of rapamycin complex 2 subunit MAPKAP1 | protein | 78 | 22% helix, 35% strand | Q9BPZ7 |
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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.67 | 0.83 | 38 | GNP, MG |
| 2 | 72 | 0.34 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 674 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7VV9 · Crystal Structure of HRas(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of… · the same entry in another collection · chain A against A, 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 C 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 P01112
- Every structure of UniProt Q9BPZ7
- Elsewhere: RCSB PDB 7VV9 · PDBe 7VV9 · UniProt P01112 · UniProt Q9BPZ7
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