Research workbench
Threonine 204 of the chaperone protein HSC70 influences the structure of the active site but is not essential for ATP hydrolysis
Analyse Threonine 204 of the chaperone protein HSC70 influences the structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ATS
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat-shock cognate 70 kd protein
- EC
- 3.6.1.3
- UniProt
- P19120
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat-shock cognate 70 kd protein (EC 3.6.1.3) | protein | 382 | 39% helix, 29% strand | P19120 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 706 | 0.78 | 0.83 | 75 | MG, ADP |
Compared structures
- 1ATS · Threonine 204 of the chaperone protein HSC70 influences the structure of the active site… · the same entry in another collection · chain A against A, TM-score 1.00
- P19120 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P19120) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P19120
- Elsewhere: RCSB PDB 1ATS · PDBe 1ATS · UniProt P19120
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