Research workbench
A novel and unique ATP hydrolysis to AMP by a human HSP70 bip
Analyse A novel and unique ATP hydrolysis to AMP by a human HSP70 bip in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N1R
- Type
- protein
- Length
- 1,212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmic reticulum chaperone bip
- EC
- 3.6.4.10
- UniProt
- P11021
- Ligands
- AMP, MG, PO4, SO4
- Pockets
- 18 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Endoplasmic reticulum chaperone bip (EC 3.6.4.10) | protein | 606 | 39% helix, 27% strand | P11021 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 14 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- GOL · Glycerol · additive · 8 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.78 | 0.91 | 44 | MG, AMP, PO4 |
| 2 | 220 | 0.77 | 0.92 | 41 | MG, AMP, PO4 |
| 3 | 521 | 0.76 | 0.84 | 52 | GOL, PO4, PEG |
| 4 | 558 | 0.74 | 0.82 | 34 | GOL |
| 5 | 203 | 0.64 | 0.84 | 29 | PO4 |
Interfaces
1 interface between chains.
- A–B · 939 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7N1R · A novel and unique ATP hydrolysis to AMP by a human Hsp70 BiP · the same entry in another collection · chain A against A, TM-score 1.00
- P11021 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P11021) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P11021
- Elsewhere: RCSB PDB 7N1R · PDBe 7N1R · UniProt P11021
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