Research workbench
Cmcb from type II cut mcp
Analyse Cmcb 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
- 7MPW
- Type
- protein
- Length
- 485 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bmc domain-containing protein
- UniProt
- Q8G9V6
- Pockets
- 5 · best druggability 0.49
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bmc domain-containing protein | protein | 84 | 42% helix, 36% strand | Q8G9V6 |
| B, D | Bmc domain-containing protein | protein | 81 | 37% helix, 38% strand | Q8G9V6 |
| C, E | Bmc domain-containing protein | protein | 79 | 38% helix, 39% strand | Q8G9V6 |
| F | Bmc domain-containing protein | protein | 81 | 41% helix, 38% strand | Q8G9V6 |
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 | 89 | 0.49 | 0.82 | 17 | empty |
| 2 | 100 | 0.40 | 0.76 | 19 | empty |
| 3 | 50 | 0.37 | 0.80 | 12 | empty |
| 4 | 95 | 0.36 | 0.74 | 18 | empty |
| 5 | 96 | 0.31 | 0.73 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–F · 787 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 774 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 734 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 729 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 609 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7MPW · CmcB 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 Q8G9V6
- Elsewhere: RCSB PDB 7MPW · PDBe 7MPW · UniProt Q8G9V6
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