MolNFT v1 · #129150 · protein
Mycoplasma genitalium dnak-nbd in complex with ATP
5OBW · Chaperone protein dnak: “Mycoplasma genitalium dnak-nbd in complex with ATP”. X-ray diffraction, 5 ligands (ADP, MG, SO4), 1 pocket (best druggability 0.72). MolNFT v1 #129150 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5OBW
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak
- UniProt
- P47547
- Ligands
- ADP, MG, SO4, PO4, SCN
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein dnak | protein | 371 | 41% helix, 28% strand | P47547 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- SCN · Thiocyanate ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · 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 | 555 | 0.72 | 0.81 | 62 | MG, ADP, PO4 |
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 P47547
- Elsewhere: RCSB PDB 5OBW · PDBe 5OBW · UniProt P47547
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