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Asymmetric hydrolysis state of HSC82 in complex with AHA1 bound with ADP and atpgammas
Analyse Asymmetric hydrolysis state of HSC82 in complex with AHA1 bound with ADP and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XLH
- Type
- protein
- Length
- 1,675 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent molecular chaperone HSC82; HSP90 co-chaperone AHA1
- UniProt
- P15108, Q12449
- Ligands
- AGS, ADP, MG, K
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 3 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP-dependent molecular chaperone HSC82 | protein | 607 | 37% helix, 21% strand | P15108 |
| C | HSP90 co-chaperone AHA1 | protein | 316 | 28% helix, 34% strand | Q12449 |
| D | HSP90 co-chaperone AHA1 | protein | 145 | 23% helix, 37% strand | Q12449 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.84 | 0.95 | 39 | AGS, MG, K |
| 2 | 290 | 0.82 | 0.93 | 38 | ADP, MG, K |
| 3 | 377 | 0.80 | 0.89 | 55 | empty |
| 4 | 82 | 0.73 | 0.97 | 32 | empty |
| 5 | 232 | 0.73 | 0.88 | 38 | empty |
Interfaces
5 interfaces between chains.
- A–B · 4353 Ų buried · 51 hydrogen bonds · protein-protein
- A–C · 1926 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 1901 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1314 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 740 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6XLH · Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS · the same entry in another collection · chain A against A, TM-score 1.00
- P15108 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSC82 (P15108) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q12449 · AlphaFold monomer V2.0 prediction for HSP90 co-chaperone AHA1 (Q12449) · a predicted model of the same protein · chain D against A, TM-score 0.95
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 P15108
- Every structure of UniProt Q12449
- Elsewhere: RCSB PDB 6XLH · PDBe 6XLH · UniProt P15108 · UniProt Q12449
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