MolNFT v1 · #134974 · protein
Crystal structure of the co-translational HSP70 chaperone ssb in the ATP-bound, open conformation
5TKY · Putative uncharacterized protein: “Crystal structure of the co-translational HSP70 chaperone ssb in the ATP-bound, open conformation”. X-ray diffraction, 2 ligands (ATP, MG), 15 pockets (best druggability 0.82). MolNFT v1 #134974 on…
- PDB
- 5TKY
- Type
- protein
- Length
- 1,188 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein
- UniProt
- G0SCU5
- Ligands
- ATP, MG
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein | protein | 597 | 39% helix, 28% strand | G0SCU5 |
| B | Putative uncharacterized protein | protein | 591 | 40% helix, 28% strand | G0SCU5 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.82 | 0.93 | 57 | ATP, MG |
| 2 | 253 | 0.82 | 0.94 | 50 | ATP, MG |
| 3 | 297 | 0.81 | 0.92 | 39 | empty |
| 4 | 676 | 0.76 | 0.82 | 66 | empty |
| 5 | 138 | 0.51 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1659 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5TKY · Crystal structure of the co-translational Hsp70 chaperone Ssb in the ATP-bound, open… · the same entry in another collection · chain A against A, TM-score 1.00
- G0SCU5 · AlphaFold monomer V2.0 prediction for ribosome-associated molecular chaperone SSB1… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 G0SCU5
- Elsewhere: RCSB PDB 5TKY · PDBe 5TKY · UniProt G0SCU5
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