Research workbench
Crystal structure of the carboxy-terminal domain of htpg, the E. COLI HSP90
Analyse Crystal structure of the carboxy-terminal 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
- 1SF8
- Type
- protein
- Length
- 932 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein htpg
- UniProt
- P0A6Z3
- Ligands
- NI, CL
- Pockets
- 15 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | Chaperone protein htpg | protein | 115 | 53% helix, 10% strand | P0A6Z3 |
| C | Chaperone protein htpg | protein | 120 | 48% helix, 13% strand | P0A6Z3 |
| G | Chaperone protein htpg | protein | 121 | 51% helix, 10% strand | P0A6Z3 |
| H | Chaperone protein htpg | protein | 116 | 54% helix, 10% strand | P0A6Z3 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 3 copies · chains C, D, G
- CL · Chloride ion · ion · 3 copies · chains E, F, B, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.77 | 0.80 | 71 | empty |
| 2 | 870 | 0.70 | 0.75 | 66 | empty |
| 3 | 222 | 0.59 | 0.80 | 26 | empty |
| 4 | 189 | 0.57 | 0.80 | 26 | empty |
| 5 | 185 | 0.50 | 0.77 | 25 | empty |
Interfaces
15 interfaces between chains.
- D–F · 946 Ų buried · 12 hydrogen bonds · protein-protein
- A–G · 935 Ų buried · 8 hydrogen bonds · protein-protein
- B–H · 933 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 914 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 550 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 1SF8 · Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90 · the same entry in another collection · chain H against H, TM-score 1.00
- P0A6Z3 · AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 1SF8 · PDBe 1SF8 · UniProt P0A6Z3
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