Research workbench
MSMEG_2027 domain-swapped dimer
Analyse MSMEG_2027 domain-swapped dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XRI
- Type
- protein
- Length
- 1,876 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- A0QU01
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, G, I, K, M | Uncharacterized protein | protein | 135 | 31% helix, 33% strand | A0QU01 |
| C, E, F, H, J | Uncharacterized protein | protein | 134 | 32% helix, 31% strand | A0QU01 |
| L | Uncharacterized protein | protein | 129 | 28% helix, 32% strand | A0QU01 |
| N | Uncharacterized protein | protein | 132 | 30% helix, 30% strand | A0QU01 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.71 | 0.75 | 101 | empty |
| 2 | 928 | 0.71 | 0.76 | 77 | empty |
| 3 | 853 | 0.68 | 0.74 | 71 | empty |
| 4 | 329 | 0.59 | 0.77 | 40 | empty |
| 5 | 218 | 0.59 | 0.80 | 27 | empty |
Interfaces
30 interfaces between chains.
- I–J · 2006 Ų buried · 29 hydrogen bonds · protein-protein
- A–F · 1991 Ų buried · 26 hydrogen bonds · protein-protein
- M–N · 1989 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 1957 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1953 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 6XRI · MSMEG_2027 domain-swapped dimer · 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 A0QU01
- Elsewhere: RCSB PDB 6XRI · PDBe 6XRI · UniProt A0QU01
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