MolNFT v1 · #175091 · protein
Cryo-EM structure of the flagellar proximal rod with flif peptides from salmonella
7CG0 · Flagellar ms ring L2: “Cryo-EM structure of the flagellar proximal rod with flif peptides from salmonella”. Electron microscopy, 20 pockets (best druggability 0.72). MolNFT v1 #175091 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7CG0
- Type
- protein
- Length
- 1,487 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar ms ring L2; Flagellar ms ring L1; Flagellar basal-body rod protein flgc…
- UniProt
- P15928, P0A1I7, P16437
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 12 distinct chains · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0, 1, 2, 3, 4 | Flagellar ms ring L2 | protein | 15 | 0% helix, 0% strand | — |
| 5, 6, 7, 9, 8 | Flagellar ms ring L1 | protein | 21 | 0% helix, 10% strand | P15928 |
| f | Flagellar basal-body rod protein flgc | protein | 128 | 47% helix, 20% strand | P0A1I7 |
| g | Flagellar basal-body rod protein flgc | protein | 130 | 49% helix, 18% strand | P0A1I7 |
| h | Flagellar basal-body rod protein flgc | protein | 128 | 44% helix, 15% strand | P0A1I7 |
| j | Flagellar basal-body rod protein flgc | protein | 127 | 48% helix, 17% strand | P0A1I7 |
| l, m | Flagellar basal body rod protein flgb | protein | 106 | 64% helix, 5% strand | P16437 |
| o | Flagellar basal body rod protein flgb | protein | 109 | 63% helix, 5% strand | P16437 |
| p | Flagellar basal-body rod protein flgc | protein | 129 | 47% helix, 18% strand | P0A1I7 |
| i | Flagellar basal-body rod protein flgc | protein | 129 | 44% helix, 16% strand | P0A1I7 |
| k | Flagellar basal body rod protein flgb | protein | 108 | 62% helix, 5% strand | P16437 |
| n | Flagellar basal body rod protein flgb | protein | 107 | 64% helix, 5% strand | P16437 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 960 | 0.72 | 0.76 | 92 | empty |
| 2 | 305 | 0.64 | 0.80 | 35 | empty |
| 3 | 507 | 0.62 | 0.75 | 54 | empty |
| 4 | 252 | 0.57 | 0.78 | 26 | empty |
| 5 | 241 | 0.56 | 0.77 | 23 | empty |
Interfaces
37 interfaces between chains.
- g–p · 1165 Ų buried · 4 hydrogen bonds · protein-protein
- i–k · 1096 Ų buried · 6 hydrogen bonds · protein-protein
- j–n · 1076 Ų buried · 5 hydrogen bonds · protein-protein
- f–l · 1052 Ų buried · 7 hydrogen bonds · protein-protein
- h–m · 1044 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7CG0 · Cryo-EM structure of the flagellar proximal rod with FliF peptides from Salmonella · the same entry in another collection · chain 9 against 9, 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
- Every structure of UniProt P0A1I7
- Every structure of UniProt P16437
- Elsewhere: RCSB PDB 7CG0 · PDBe 7CG0 · UniProt P15928 · UniProt P0A1I7 · UniProt P16437
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