MolNFT v1 · #163778 · protein
Structure of the RBM3/COLLAR region of the salmonella flagella ms-ring protein flif with 33-fold symmetry applied
6SD1 · Flagellar M-ring protein: “Structure of the RBM3/COLLAR region of the salmonella flagella ms-ring protein flif with 33-fold symmetry…”. Electron microscopy, 20 pockets (best druggability 0.72). MolNFT v1 #163778 on GenesisL1: 3D…
- PDB
- 6SD1
- Type
- protein
- Length
- 4,983 residues
- Chains
- 33
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein
- UniProt
- P15928
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 26% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g | Flagellar M-ring protein | protein | 151 | 26% helix, 41% strand | P15928 |
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 | 235 | 0.72 | 0.88 | 34 | empty |
| 2 | 289 | 0.71 | 0.85 | 39 | empty |
| 3 | 256 | 0.71 | 0.86 | 33 | empty |
| 4 | 212 | 0.71 | 0.87 | 28 | empty |
| 5 | 269 | 0.71 | 0.86 | 35 | empty |
Interfaces
33 interfaces between chains.
- T–U · 2307 Ų buried · 48 hydrogen bonds · protein-protein
- W–X · 2304 Ų buried · 47 hydrogen bonds · protein-protein
- O–P · 2304 Ų buried · 46 hydrogen bonds · protein-protein
- L–M · 2304 Ų buried · 44 hydrogen bonds · protein-protein
- X–Y · 2299 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 6SD1 · Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with… · the same entry in another collection · chain J against J, 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 6SD1 · PDBe 6SD1 · UniProt P15928
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