MolNFT v1 · #64828 · protein
Faee-faeg chaperone-major pilin complex of F4 ad fimbriae
3GEW: “Faee-faeg chaperone-major pilin complex of F4 ad fimbriae”. X-ray diffraction. MolNFT v1 #64828 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3GEW
- Type
- protein
- Length
- 839 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25401, P14191
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 199 | — | P25401 |
| C | — | protein | 208 | — | P25401 |
| D | — | protein | 217 | — | P14191 |
| A | — | protein | 215 | — | P14191 |
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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