Research workbench
The F4 fimbrial chaperone faee does not self-cap its interactive surfaces
Analyse The F4 fimbrial chaperone faee does not self-cap its interactive surfaces in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F65
- Type
- protein
- Length
- 1,484 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein faee
- UniProt
- P25401
- Ligands
- PO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 7 distinct chains · 5% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Chaperone protein faee | protein | 206 | 7% helix, 46% strand | P25401 |
| B | Chaperone protein faee | protein | 205 | 7% helix, 46% strand | P25401 |
| D | Chaperone protein faee | protein | 161 | 4% helix, 42% strand | P25401 |
| E | Chaperone protein faee | protein | 194 | 6% helix, 43% strand | P25401 |
| F | Chaperone protein faee | protein | 166 | 5% helix, 43% strand | P25401 |
| G | Chaperone protein faee | protein | 193 | 2% helix, 46% strand | P25401 |
| H | Chaperone protein faee | protein | 153 | 4% helix, 43% strand | P25401 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, C, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 904 | 0.78 | 0.81 | 95 | empty |
| 2 | 1062 | 0.78 | 0.80 | 94 | empty |
| 3 | 955 | 0.78 | 0.80 | 94 | empty |
| 4 | 639 | 0.70 | 0.78 | 64 | empty |
| 5 | 949 | 0.69 | 0.74 | 84 | empty |
Interfaces
13 interfaces between chains.
- A–D · 728 Ų buried · 15 hydrogen bonds · protein-protein
- E–H · 715 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 636 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 614 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 600 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3F65 · The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces · the same entry in another collection · chain H against H, TM-score 1.00
- P25401 · AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) · a predicted model of the same protein · chain E against A, TM-score 0.97
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 P25401
- Elsewhere: RCSB PDB 3F65 · PDBe 3F65 · UniProt P25401
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