Research workbench
Molecular basis for SHROOM2 recognition by ROCK1
Analyse Molecular basis for SHROOM2 recognition by ROCK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F5P
- Type
- protein
- Length
- 934 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein SHROOM2; Rho-associated protein kinase 1
- EC
- 2.7.11.1
- UniProt
- Q13796, Q13464
- Ligands
- CL
- Pockets
- 18 · best druggability 0.64
Structure
x-ray diffraction · 8 distinct chains · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein SHROOM2 | protein | 181 | 93% helix, 0% strand | Q13796 |
| B | Protein SHROOM2 | protein | 171 | 94% helix, 0% strand | Q13796 |
| C | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 55 | 93% helix, 0% strand | Q13464 |
| D | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 61 | 97% helix, 0% strand | Q13464 |
| E | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 57 | 96% helix, 0% strand | Q13464 |
| F | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 58 | 95% helix, 0% strand | Q13464 |
| G | Protein SHROOM2 | protein | 180 | 92% helix, 0% strand | Q13796 |
| H | Protein SHROOM2 | protein | 171 | 94% helix, 0% strand | Q13796 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 567 | 0.64 | 0.75 | 72 | empty |
| 2 | 142 | 0.58 | 0.83 | 26 | empty |
| 3 | 125 | 0.44 | 0.77 | 23 | CL |
| 4 | 83 | 0.42 | 0.79 | 20 | empty |
| 5 | 112 | 0.42 | 0.76 | 15 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1390 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 1305 Ų buried · 6 hydrogen bonds · protein-protein
- E–G · 964 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 945 Ų buried · 9 hydrogen bonds · protein-protein
- F–H · 891 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 Q13796
- Every structure of UniProt Q13464
- Elsewhere: RCSB PDB 5F5P · PDBe 5F5P · UniProt Q13796 · UniProt Q13464
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