Research workbench
Structure of the major type 1 pilus subunit fima bound to the fimc (2.5 a resolution)
Analyse Structure of the major type 1 pilus subunit fima bound to the fimc (2.5 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DWH
- Type
- protein
- Length
- 665 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P31697, P04128
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 197 | — | P31697 |
| B | — | protein | 133 | — | P04128 |
| C | — | protein | 201 | — | P31697 |
| D | — | protein | 134 | — | P04128 |
Compared structures
- 4DWH · Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution) · the same entry in another collection · chain D against D, TM-score 1.00
- P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P04128 · AlphaFold monomer V2.0 prediction for type-1 fimbrial protein, a chain (P04128) · a predicted model of the same protein · chain D against A, TM-score 0.85
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 P31697
- Every structure of UniProt P04128
- Elsewhere: RCSB PDB 4DWH · PDBe 4DWH · UniProt P31697 · UniProt P04128
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