Research workbench
Mxid N0 N1 and mxig C-terminal domains of the shigella type 3 secretion system
Analyse Mxid N0 N1 and mxig C-terminal domains of the shigella type 3 secretion system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RWK
- Type
- protein
- Length
- 2,688 residues
- Chains
- 32
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane protein mxid; Protein mxig
- UniProt
- Q04641, P0A221
- Pockets
- 20 · best druggability 0.57
Structure
electron microscopy · 2 distinct chains · 30% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X, Y, Z, 0, 2, 4, 6, 8, x, y, z, 1, 3, 5, 7, 9 | Outer membrane protein mxid | protein | 138 | 37% helix, 31% strand | Q04641 |
| A, D, G, J, M, P, S, U, B, E, H, K, N, Q, T, V | Protein mxig | protein | 30 | 0% helix, 40% strand | P0A221 |
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 | 177 | 0.57 | 0.81 | 28 | empty |
| 2 | 81 | 0.56 | 0.86 | 21 | empty |
| 3 | 81 | 0.56 | 0.86 | 20 | empty |
| 4 | 92 | 0.56 | 0.85 | 20 | empty |
| 5 | 261 | 0.55 | 0.77 | 35 | empty |
Interfaces
48 interfaces between chains.
- 8–7 · 1100 Ų buried · 14 hydrogen bonds · protein-protein
- Z–y · 1096 Ų buried · 14 hydrogen bonds · protein-protein
- X–9 · 1094 Ų buried · 14 hydrogen bonds · protein-protein
- 4–3 · 1094 Ų buried · 14 hydrogen bonds · protein-protein
- 2–1 · 1093 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6RWK · MxiD N0 N1 and MxiG C-terminal domains of the Shigella type 3 secretion system · the same entry in another collection · chain z against z, 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 Q04641
- Every structure of UniProt P0A221
- Elsewhere: RCSB PDB 6RWK · PDBe 6RWK · UniProt Q04641 · UniProt P0A221
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