Research workbench
Type VI membrane complex
Analyse Type VI membrane complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HS7
- Type
- protein
- Length
- 6,905 residues
- Chains
- 25
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imcf-like family protein; Type VI secretion system protein vasd
- UniProt
- I2W7L4, H4UNW1
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 3 distinct chains · 37% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Imcf-like family protein | protein | 478 | 42% helix, 8% strand | I2W7L4 |
| F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | Type VI secretion system protein vasd | protein | 130 | 8% helix, 45% strand | H4UNW1 |
| a, b, c, d, e | Imcf-like family protein | protein | 513 | 40% helix, 9% strand | I2W7L4 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.86 | 0.88 | 114 | empty |
| 2 | 885 | 0.86 | 0.88 | 114 | empty |
| 3 | 797 | 0.85 | 0.88 | 91 | empty |
| 4 | 746 | 0.84 | 0.88 | 89 | empty |
| 5 | 1182 | 0.84 | 0.85 | 118 | empty |
Interfaces
55 interfaces between chains.
- a–e · 1664 Ų buried · 20 hydrogen bonds · protein-protein
- a–b · 1648 Ų buried · 16 hydrogen bonds · protein-protein
- c–d · 1641 Ų buried · 16 hydrogen bonds · protein-protein
- d–e · 1622 Ų buried · 17 hydrogen bonds · protein-protein
- b–c · 1621 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6HS7 · Type VI membrane complex · the same entry in another collection · chain B against B, 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 I2W7L4
- Every structure of UniProt H4UNW1
- Elsewhere: RCSB PDB 6HS7 · PDBe 6HS7 · UniProt I2W7L4 · UniProt H4UNW1
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