MolNFT v1 · #129328 · protein
The cryo-electron microscopy structure of the type 1 chaperone-usher pilus rod
5OH0: “The cryo-electron microscopy structure of the type 1 chaperone-usher pilus rod”. Electron microscopy. MolNFT v1 #129328 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OH0
- Type
- protein
- Length
- 942 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04128
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 157 | — | P04128 |
Compared structures
- 5OH0 · The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod · the same entry in another collection · chain F against F, TM-score 1.00
- P04128 · AlphaFold monomer V2.0 prediction for type-1 fimbrial protein, a chain (P04128) · a predicted model of the same protein · chain E against A, TM-score 0.93
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 P04128
- Elsewhere: RCSB PDB 5OH0 · PDBe 5OH0 · UniProt P04128
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