Research workbench
Structure of the RBM2INNER region of the salmonella flagella ms-ring protein flif with 21-fold symmetry applied.
Analyse Structure of the RBM2INNER region of the salmonella flagella ms-ring protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SD2
- Type
- protein
- Length
- 1,848 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein
- UniProt
- P15928
- Pockets
- 20 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, G, I, J, L, N, O, Q, R, T, U, W, Y, Z, b, c, e, f | Flagellar M-ring protein | protein | 88 | 36% helix, 22% strand | P15928 |
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.68 | 0.78 | 82 | empty |
| 2 | 483 | 0.67 | 0.78 | 82 | empty |
| 3 | 429 | 0.66 | 0.78 | 68 | empty |
| 4 | 324 | 0.62 | 0.78 | 58 | empty |
| 5 | 121 | 0.46 | 0.79 | 22 | empty |
Interfaces
21 interfaces between chains.
- A–C · 861 Ų buried · 6 hydrogen bonds · protein-protein
- R–T · 859 Ų buried · 8 hydrogen bonds · protein-protein
- e–f · 852 Ų buried · 7 hydrogen bonds · protein-protein
- c–e · 850 Ų buried · 4 hydrogen bonds · protein-protein
- G–I · 850 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6SD2 · Structure of the RBM2inner region of the Salmonella flagella MS-ring protein FliF with… · the same entry in another collection · chain Q against Q, 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 P15928
- Elsewhere: RCSB PDB 6SD2 · PDBe 6SD2 · UniProt P15928
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