Research workbench
Crystal structure and functional implications of the tandem-type universal stress protein uspe from escherichia COLI
Analyse Crystal structure and functional implications of the tandem-type universal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CB0
- Type
- protein
- Length
- 578 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AAC0
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 290 | — | P0AAC0 |
| B | — | protein | 288 | — | P0AAC0 |
Compared structures
- P0AAC0 · AlphaFold monomer V2.0 prediction for universal stress protein E (P0AAC0) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P0AAC0
- Elsewhere: RCSB PDB 5CB0 · PDBe 5CB0 · UniProt P0AAC0
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