MolNFT v1 · #154071 · protein
Structural characterization of dnaj from streptococcus pneumonia presents a new tetramer of HSP40 family
6JZB · Chaperone protein dnaj: “Structural characterization of dnaj from streptococcus pneumonia presents a new tetramer of HSP40 family”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.28). MolNFT v1 #154071 on GenesisL1…
- PDB
- 6JZB
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnaj
- UniProt
- A0MSU1
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein dnaj | protein | 251 | 10% helix, 35% strand | A0MSU1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.28 | 0.73 | 16 | empty |
Compared structures
- 6JZB · Structural characterization of DnaJ from Streptococcus pneumonia presents a new tetramer… · 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 A0MSU1
- Elsewhere: RCSB PDB 6JZB · PDBe 6JZB · UniProt A0MSU1
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