Research workbench
Crystal structure of human mc-HSP90 in P21 space group
Analyse Crystal structure of human mc-HSP90 in P21 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q6N
- Type
- protein
- Length
- 2,159 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP 90-alpha
- UniProt
- P07900
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.70
Structure
x-ray diffraction · 6 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP 90-alpha | protein | 360 | 42% helix, 18% strand | P07900 |
| B | Heat shock protein HSP 90-alpha | protein | 362 | 42% helix, 18% strand | P07900 |
| C | Heat shock protein HSP 90-alpha | protein | 354 | 43% helix, 19% strand | P07900 |
| D | Heat shock protein HSP 90-alpha | protein | 360 | 43% helix, 18% strand | P07900 |
| E | Heat shock protein HSP 90-alpha | protein | 360 | 43% helix, 18% strand | P07900 |
| F | Heat shock protein HSP 90-alpha | protein | 363 | 44% helix, 18% strand | P07900 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.70 | 0.81 | 63 | empty |
| 2 | 351 | 0.68 | 0.81 | 57 | empty |
| 3 | 417 | 0.63 | 0.77 | 43 | empty |
| 4 | 324 | 0.60 | 0.78 | 36 | empty |
| 5 | 142 | 0.59 | 0.84 | 34 | empty |
Interfaces
10 interfaces between chains.
- A–B · 1310 Ų buried · 4 hydrogen bonds · protein-protein
- E–F · 1302 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 1256 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 344 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 329 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3Q6N · Crystal Structure of Human MC-HSP90 in P21 space group · 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 P07900
- Elsewhere: RCSB PDB 3Q6N · PDBe 3Q6N · UniProt P07900
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