MolNFT v1 · #163781 · protein
Structure of the RBM3/COLLAR region of the salmonella flagella ms-ring protein flif with 34-fold symmetry applied
6SD4 · Flagellar M-ring protein: “Structure of the RBM3/COLLAR region of the salmonella flagella ms-ring protein flif with 34-fold symmetry…”. Electron microscopy, 20 pockets (best druggability 0.82). MolNFT v1 #163781 on GenesisL1: 3D…
- PDB
- 6SD4
- Type
- protein
- Length
- 5,134 residues
- Chains
- 34
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein
- UniProt
- P15928
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 28% helix, 33% 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, h | Flagellar M-ring protein | protein | 151 | 28% helix, 33% 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 | 1002 | 0.82 | 0.83 | 114 | empty |
| 2 | 902 | 0.82 | 0.84 | 115 | empty |
| 3 | 866 | 0.82 | 0.84 | 101 | empty |
| 4 | 904 | 0.81 | 0.84 | 111 | empty |
| 5 | 511 | 0.80 | 0.87 | 69 | empty |
Interfaces
34 interfaces between chains.
- X–Y · 2279 Ų buried · 40 hydrogen bonds · protein-protein
- f–g · 2274 Ų buried · 41 hydrogen bonds · protein-protein
- F–G · 2271 Ų buried · 42 hydrogen bonds · protein-protein
- M–N · 2260 Ų buried · 39 hydrogen bonds · protein-protein
- c–d · 2260 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 6SD4 · Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with… · the same entry in another collection · chain K against K, 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 6SD4 · PDBe 6SD4 · UniProt P15928
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