Research workbench
Crystal structure of the E. COLI chaperone drab
Analyse Crystal structure of the E. COLI chaperone drab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DJM
- Type
- protein
- Length
- 1,609 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7BG37
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 197 | — | Q7BG37 |
| B, F | — | protein | 203 | — | Q7BG37 |
| C, G | — | protein | 200 | — | Q7BG37 |
| D | — | protein | 205 | — | Q7BG37 |
| E | — | protein | 199 | — | Q7BG37 |
| H | — | protein | 202 | — | Q7BG37 |
Compared structures
- 4DJM · Crystal structure of the E. coli chaperone DraB · the same entry in another collection · chain A against A, TM-score 1.00
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 Q7BG37
- Elsewhere: RCSB PDB 4DJM · PDBe 4DJM · UniProt Q7BG37
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