MolNFT v1 · #15815 · protein
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity, II. structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
1NGB · Heat-shock cognate 70 kd protein: “Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity, II. structure of…”. X-ray diffraction, 3 ligands (ADP, MG, PO4), 2 pockets (best druggability 0.77). MolNFT…
- PDB
- 1NGB
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat-shock cognate 70 kd protein
- EC
- 3.6.1.3
- UniProt
- P19120
- Ligands
- ADP, MG, PO4
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat-shock cognate 70 kd protein (EC 3.6.1.3) | protein | 378 | 40% helix, 29% strand | P19120 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.77 | 0.83 | 70 | MG, PO4, ADP |
| 2 | 52 | 0.43 | 0.83 | 13 | empty |
Compared structures
- 1NGB · Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity… · the same entry in another collection · chain A against A, TM-score 1.00
- P19120 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P19120) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P19120
- Elsewhere: RCSB PDB 1NGB · PDBe 1NGB · UniProt P19120
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