Research workbench
I-layer structure (TRWF/VIRB9NTD, TRWE/VIRB10NTD) of the outer membrane core complex from the fully-assembled R388 type IV secretion system determined by cryo-EM.
Analyse I-layer structure (TRWF/VIRB9NTD, TRWE/VIRB10NTD) of the outer membrane core… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O3T
- Type
- protein
- Length
- 2,144 residues
- Chains
- 32
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trwe protein; Trwf protein
- UniProt
- O50337, O50336
- Pockets
- 20 · best druggability 0.44
Structure
electron microscopy · 2 distinct chains · 13% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J, M, P, S, u, V, Y, b, e, h, k, n, y | Trwe protein | protein | 19 | 58% helix, 0% strand | O50337 |
| B, E, H, K, N, Q, T, v, W, Z, c, f, i, l, o, z | Trwf protein | protein | 115 | 6% helix, 45% strand | O50336 |
Pockets
20 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.44 | 0.79 | 24 | empty |
| 2 | 91 | 0.44 | 0.79 | 25 | empty |
| 3 | 100 | 0.43 | 0.78 | 21 | empty |
| 4 | 94 | 0.43 | 0.79 | 22 | empty |
| 5 | 55 | 0.40 | 0.82 | 16 | empty |
Interfaces
48 interfaces between chains.
- N–Q · 802 Ų buried · 6 hydrogen bonds · protein-protein
- c–f · 800 Ų buried · 5 hydrogen bonds · protein-protein
- i–l · 799 Ų buried · 6 hydrogen bonds · protein-protein
- H–K · 798 Ų buried · 6 hydrogen bonds · protein-protein
- B–z · 798 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7O3T · I-layer structure (TrwF/VirB9NTD, TrwE/VirB10NTD) of the outer membrane core complex from… · 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 O50337
- Every structure of UniProt O50336
- Elsewhere: RCSB PDB 7O3T · PDBe 7O3T · UniProt O50337 · UniProt O50336
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