MolNFT v1 · #175825 · protein
Crystal structure of RSU1/PINCH1_LIM5C complex
7D2S · RAS suppressor protein 1: “Crystal structure of RSU1/PINCH1_LIM5C complex”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.72). MolNFT v1 #175825 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7D2S
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS suppressor protein 1; Lim and senescent cell antigen-like-containing domain protein 1
- UniProt
- Q15404, P48059
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS suppressor protein 1 | protein | 206 | 23% helix, 13% strand | Q15404 |
| B | Lim and senescent cell antigen-like-containing domain protein 1 | protein | 70 | 20% helix, 29% strand | P48059 |
Ligands and binding sites
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 | 193 | 0.72 | 0.89 | 27 | empty |
| 2 | 53 | 0.33 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1056 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7D2S · Crystal structure of Rsu1/PINCH1_LIM5C complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q15404 · AlphaFold monomer V2.0 prediction for RAS suppressor protein 1 (Q15404) · a predicted model of the same protein · chain A against A, TM-score 0.97
- P48059 · AlphaFold monomer V2.0 prediction for lim and senescent cell antigen- like-containing… · a predicted model of the same protein · chain B against A, TM-score 0.89
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 Q15404
- Every structure of UniProt P48059
- Elsewhere: RCSB PDB 7D2S · PDBe 7D2S · UniProt Q15404 · UniProt P48059
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