Research workbench
Dsba mutant P151A, role of the cis-proline in the active site of dsba
Analyse Dsba mutant P151A, role of the cis-proline in the active site of dsba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BQ7
- Type
- protein
- Length
- 1,116 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (disulfide oxidoreductase)
- UniProt
- P24991
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Protein (disulfide oxidoreductase) | protein | 186 | 53% helix, 11% strand | P24991 |
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1065 | 0.75 | 0.77 | 94 | empty |
| 2 | 435 | 0.66 | 0.79 | 45 | empty |
| 3 | 296 | 0.63 | 0.80 | 37 | empty |
| 4 | 402 | 0.61 | 0.76 | 38 | empty |
| 5 | 355 | 0.58 | 0.76 | 40 | empty |
Interfaces
9 interfaces between chains.
- D–F · 934 Ų buried · 9 hydrogen bonds · protein-protein
- C–F · 526 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 520 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 271 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 232 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1BQ7 · Dsba mutant P151A, role of the cis-proline in the active site of 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 1BQ7 · PDBe 1BQ7 · UniProt P24991
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