Research workbench
Crystal structure of the stress-inducible human heat shock protein HSP70 substrate-binding domain in complex with peptide substrate
Analyse Crystal structure of the stress-inducible human heat shock protein HSP70… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PO2
- Type
- protein
- Length
- 456 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock 70 kda protein 1A/1B; HSP70 substrate peptide
- UniProt
- P08107
- Ligands
- SO4, PO4
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock 70 kda protein 1A/1B | protein | 228 | 43% helix, 27% strand | P08107 |
| B | Heat shock 70 kda protein 1A/1B | protein | 215 | 41% helix, 28% strand | P08107 |
| C | HSP70 substrate peptide | protein | 7 | 0% helix, 29% strand | — |
| D | HSP70 substrate peptide | protein | 6 | 0% helix, 33% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 816 | 0.68 | 0.75 | 85 | PO4, SO4 |
| 2 | 92 | 0.51 | 0.82 | 17 | empty |
| 3 | 101 | 0.37 | 0.75 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 757 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 611 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 597 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4PO2 · Crystal Structure of the Stress-Inducible Human Heat Shock Protein HSP70… · 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 P08107
- Elsewhere: RCSB PDB 4PO2 · PDBe 4PO2 · UniProt P08107
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