Research workbench
Faee-faeg chaperone-major pilin complex of F4 ad fimbriae
Analyse Faee-faeg chaperone-major pilin complex of F4 ad fimbriae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GEW
- Type
- protein
- Length
- 839 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein faee; K88 fimbrial protein ad
- UniProt
- P25401, P14191
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Chaperone protein faee | protein | 199 | 7% helix, 45% strand | P25401 |
| C | Chaperone protein faee | protein | 208 | 7% helix, 44% strand | P25401 |
| D | K88 fimbrial protein ad | protein | 217 | 12% helix, 41% strand | P14191 |
| A | K88 fimbrial protein ad | protein | 215 | 10% helix, 42% strand | P14191 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains B, C, D, A
- GOL · Glycerol · additive · 2 copies · chains C, D, B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 614 | 0.70 | 0.78 | 64 | SO4 |
| 2 | 618 | 0.69 | 0.78 | 62 | SO4 |
| 3 | 207 | 0.67 | 0.85 | 36 | empty |
| 4 | 277 | 0.59 | 0.78 | 43 | empty |
| 5 | 240 | 0.56 | 0.78 | 36 | empty |
Interfaces
5 interfaces between chains.
- B–A · 1532 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 1509 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 699 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 157 Ų buried · 2 hydrogen bonds · protein-protein
- C–A · 134 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3GEW · FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae · the same entry in another collection · chain A against A, TM-score 1.00
- P25401 · AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) · a predicted model of the same protein · chain B against A, TM-score 1.00
- P14191 · AlphaFold monomer V2.0 prediction for K88 fimbrial protein ad (P14191) · a predicted model of the same protein · chain A against A, TM-score 0.96
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
- Every structure of UniProt P14191
- Elsewhere: RCSB PDB 3GEW · PDBe 3GEW · UniProt P25401 · UniProt P14191
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