Research workbench
Structure of the RBM2 inner ring of salmonella flagella ms-ring protein flif with 22-fold symmetry applied
Analyse Structure of the RBM2 inner ring of salmonella flagella ms-ring protein flif… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SD5
- Type
- protein
- Length
- 1,936 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein
- UniProt
- P15928
- Pockets
- 13 · best druggability 0.65
Structure
electron microscopy · 1 distinct chain · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, G, I, J, L, M, O, P, R, T, U, W, X, Z, a, c, d, f, g | Flagellar M-ring protein | protein | 88 | 32% helix, 17% strand | P15928 |
Pockets
13 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 615 | 0.65 | 0.75 | 107 | empty |
| 2 | 587 | 0.63 | 0.74 | 107 | empty |
| 3 | 218 | 0.50 | 0.75 | 43 | empty |
| 4 | 173 | 0.46 | 0.75 | 30 | empty |
| 5 | 62 | 0.35 | 0.78 | 13 | empty |
Interfaces
22 interfaces between chains.
- F–G · 905 Ų buried · 5 hydrogen bonds · protein-protein
- a–c · 904 Ų buried · 5 hydrogen bonds · protein-protein
- f–g · 904 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 903 Ų buried · 5 hydrogen bonds · protein-protein
- c–d · 901 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6SD5 · Structure of the RBM2 inner ring of Salmonella flagella MS-ring protein FliF with 22-fold… · the same entry in another collection · chain P against P, 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 6SD5 · PDBe 6SD5 · UniProt P15928
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