Research workbench
Hslv-hslu from E.COLI
Analyse Hslv-hslu from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E94
- Type
- protein
- Length
- 1,512 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein hslv; Heat shock protein hslu
- UniProt
- P31059, P32168
- Ligands
- ANP
- Pockets
- 11 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Heat shock protein hslv | protein | 174 | 34% helix, 31% strand | P31059 |
| E, F | Heat shock protein hslu | protein | 408 | 54% helix, 11% strand | P32168 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.87 | 0.88 | 101 | ANP |
| 2 | 630 | 0.69 | 0.77 | 72 | empty |
| 3 | 524 | 0.65 | 0.76 | 59 | empty |
| 4 | 255 | 0.58 | 0.79 | 35 | ANP |
| 5 | 477 | 0.57 | 0.73 | 54 | empty |
Interfaces
5 interfaces between chains.
- E–F · 2430 Ų buried · 31 hydrogen bonds · protein-protein
- A–B · 454 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 400 Ų buried · 3 hydrogen bonds · protein-protein
- B–F · 336 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 263 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1E94 · HslV-HslU from E.coli · 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 P31059
- Every structure of UniProt P32168
- Elsewhere: RCSB PDB 1E94 · PDBe 1E94 · UniProt P31059 · UniProt P32168
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