Research workbench
The 1.7 ångström structure of wild type disulfide bond formation protein (dsba)
Analyse The 1.7 ångström structure of wild type disulfide bond formation protein (dsba) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FVK
- Type
- protein
- Length
- 376 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disulfide bond formation protein
- UniProt
- P24991
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Disulfide bond formation protein | 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 | 358 | 0.62 | 0.78 | 57 | empty |
| 2 | 87 | 0.33 | 0.74 | 14 | empty |
| 3 | 60 | 0.30 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 804 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1FVK · The 1.7 ångström structure of wild type disulfide bond formation protein (dsba) · 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 1FVK · PDBe 1FVK · UniProt P24991
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