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Crystal structure of the middle domain of htpg, the E. COLI HSP90
Analyse Crystal structure of the middle domain of htpg, the E. COLI HSP90 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GQ0
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein htpg
- EC
- 3.6.4.10
- UniProt
- P0A6Z3
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg (EC 3.6.4.10) | protein | 256 | 41% helix, 20% strand | P0A6Z3 |
| B | Chaperone protein htpg (EC 3.6.4.10) | protein | 264 | 41% helix, 20% strand | P0A6Z3 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.70 | 0.83 | 44 | empty |
| 2 | 409 | 0.58 | 0.75 | 34 | empty |
| 3 | 96 | 0.41 | 0.78 | 24 | empty |
| 4 | 79 | 0.40 | 0.79 | 21 | empty |
| 5 | 55 | 0.28 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 642 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 P0A6Z3
- Elsewhere: RCSB PDB 2GQ0 · PDBe 2GQ0 · UniProt P0A6Z3
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