Research workbench
Crystal structure of the dsba protein required for disulphide bond formation in vivo
Analyse Crystal structure of the dsba protein required for disulphide bond formation in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DSB
- Type
- protein
- Length
- 376 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dsba
- UniProt
- P24991
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dsba | protein | 188 | 54% helix, 11% strand | P24991 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.63 | 0.78 | 60 | empty |
| 2 | 126 | 0.39 | 0.74 | 18 | empty |
| 3 | 106 | 0.38 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 795 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1DSB · Crystal structure of the dsba protein required for disulphide bond formation in vivo · 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 P24991
- Elsewhere: RCSB PDB 1DSB · PDBe 1DSB · UniProt P24991
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