Research workbench
Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
Analyse Fragment-based screening of HSP70 sheds light on the functional role of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AQJ
- Type
- protein
- Length
- 1,481 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11142, Q99933
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 381 | — | P11142 |
| B | — | protein | 114 | — | Q99933 |
| D | — | protein | 112 | — | Q99933 |
| E | — | protein | 382 | — | P11142 |
| F | — | protein | 111 | — | Q99933 |
Compared structures
- Q99933 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 1 (Q99933) · a predicted model of the same protein · chain D against A, TM-score 0.93
- P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 P11142
- Every structure of UniProt Q99933
- Elsewhere: RCSB PDB 5AQJ · PDBe 5AQJ · UniProt P11142 · UniProt Q99933
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