Research workbench
Cmcc E36G mutant from type II cut mcp
Analyse Cmcc E36G mutant from type II cut mcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MPX
- Type
- protein
- Length
- 482 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bmc domain-containing protein
- UniProt
- Q8G9V7
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.42
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | Bmc domain-containing protein | protein | 80 | 40% helix, 39% strand | Q8G9V7 |
| B, E | Bmc domain-containing protein | protein | 80 | 40% helix, 39% strand | Q8G9V7 |
| C, D | Bmc domain-containing protein | protein | 81 | 40% helix, 41% strand | Q8G9V7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.42 | 0.82 | 14 | empty |
| 2 | 52 | 0.40 | 0.81 | 18 | empty |
| 3 | 59 | 0.34 | 0.76 | 13 | empty |
| 4 | 55 | 0.32 | 0.76 | 17 | empty |
| 5 | 91 | 0.31 | 0.73 | 21 | PO4 |
Interfaces
6 interfaces between chains.
- A–F · 691 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 673 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 670 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 664 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 664 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7MPX · CmcC E36G mutant from Type II Cut MCP · the same entry in another collection · chain A against A, 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 Q8G9V7
- Elsewhere: RCSB PDB 7MPX · PDBe 7MPX · UniProt Q8G9V7
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