Research workbench
Crystal structure of ADP and pi bound human HSP70 nbd mutant R272K.
Analyse Crystal structure of ADP and pi bound human HSP70 nbd mutant R272K. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BPL
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock 70 kda protein 1A
- UniProt
- P0DMV8
- Ligands
- ADP, NA, MG, PO4, CL
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock 70 kda protein 1A | protein | 380 | 39% helix, 28% strand | P0DMV8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A
- CL · Chloride ion · ion · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 701 | 0.76 | 0.81 | 79 | ADP, PO4, MG, NA, CL |
Compared structures
- P0DMV8 · AlphaFold monomer V2.0 prediction for heat shock 70 kda protein 1A (P0DMV8) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P0DMV8
- Elsewhere: RCSB PDB 5BPL · PDBe 5BPL · UniProt P0DMV8
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