Research workbench
Crystal structure of full-length htpg, the escherichia COLI HSP90, bound to ADP
Analyse Crystal structure of full-length htpg, the escherichia COLI HSP90, bound to ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IOP
- Type
- protein
- Length
- 2,443 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein htpg
- UniProt
- P0A6Z3
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 618 | 40% helix, 20% strand | P0A6Z3 |
| B | Chaperone protein htpg | protein | 615 | 39% helix, 21% strand | P0A6Z3 |
| C | Chaperone protein htpg | protein | 606 | 40% helix, 19% strand | P0A6Z3 |
| D | Chaperone protein htpg | protein | 604 | 40% helix, 20% strand | P0A6Z3 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.83 | 0.84 | 151 | empty |
| 2 | 641 | 0.82 | 0.87 | 97 | empty |
| 3 | 405 | 0.80 | 0.89 | 57 | empty |
| 4 | 752 | 0.76 | 0.81 | 79 | ADP |
| 5 | 639 | 0.76 | 0.82 | 69 | ADP |
Interfaces
6 interfaces between chains.
- B–C · 3120 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 3111 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1378 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1361 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1316 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2IOP · Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP · the same entry in another collection · chain D against D, TM-score 1.00
- P0A6Z3 · AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3) · a predicted model of the same protein · chain C against A, TM-score 0.63
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 2IOP · PDBe 2IOP · UniProt P0A6Z3
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