MolNFT v1 · #117470 · protein
Crystal structure of MB(NS1)/H-RAS complex
5E95: “Crystal structure of MB(NS1)/H-RAS complex”. X-ray diffraction, 2 ligands (GDP, MG), 3 pockets (best druggability 0.40). MolNFT v1 #117470 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5E95
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MB(NS1); GTPase HRAS
- UniProt
- P01112
- Ligands
- GDP, MG
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | MB(NS1) | protein | 92 | 0% helix, 63% strand | — |
| A | GTPase HRAS | protein | 168 | 36% helix, 24% strand | P01112 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.40 | 0.75 | 23 | empty |
| 2 | 92 | 0.36 | 0.75 | 19 | GDP, MG |
| 3 | 110 | 0.35 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- B–A · 604 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5E95 · Crystal Structure of Mb(NS1)/H-Ras Complex · the same entry in another collection · chain B against B, 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 P01112
- Elsewhere: RCSB PDB 5E95 · PDBe 5E95 · UniProt P01112
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