Research workbench
Crystal structure of the substrate binding domain of E.COLI dnak in complex with sheep BAC7(35-43)
Analyse Crystal structure of the substrate binding domain of E.COLI dnak in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JWI
- Type
- protein
- Length
- 445 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6Y8, P50415
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 213 | — | P0A6Y8 |
| B | — | protein | 216 | — | P0A6Y8 |
| C, D | — | protein | 8 | — | P50415 |
Compared structures
- 4JWI · Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep… · the same entry in another collection · chain D against D, TM-score 1.00
- P50415 · AlphaFold monomer V2.0 prediction for cathelicidin-3 (P50415) · a predicted model of the same protein · chain C against A, TM-score 0.48
- P0A6Y8 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (P0A6Y8) · a predicted model of the same protein · chain A against A, TM-score 0.47
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 P0A6Y8
- Every structure of UniProt P50415
- Elsewhere: RCSB PDB 4JWI · PDBe 4JWI · UniProt P0A6Y8 · UniProt P50415
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