Research workbench
Human HSP27 core domain in complex with C-terminal peptide
Analyse Human HSP27 core domain in complex with C-terminal peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MJH
- Type
- protein
- Length
- 180 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein beta-1
- UniProt
- P04792
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein beta-1 | protein | 86 | 3% helix, 59% strand | P04792 |
| B, D | Heat shock protein beta-1 | protein | 7 | 0% helix, 14% strand | P04792 |
| C | Heat shock protein beta-1 | protein | 80 | 4% helix, 58% strand | P04792 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.68 | 0.82 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–C · 766 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 418 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 411 Ų buried · 6 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 P04792
- Elsewhere: RCSB PDB 4MJH · PDBe 4MJH · UniProt P04792
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