Research workbench
Crystal structure of SCO6571 from streptomyces coelicolor A3(2)
Analyse Crystal structure of SCO6571 from streptomyces coelicolor A3(2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZDS
- Type
- protein
- Length
- 1,930 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative DNA-binding protein
- UniProt
- O69946
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Putative DNA-binding protein | protein | 321 | 46% helix, 15% strand | O69946 |
| B, C, D, F | Putative DNA-binding protein | protein | 322 | 46% helix, 14% strand | O69946 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.75 | 0.95 | 26 | empty |
| 2 | 65 | 0.73 | 0.97 | 24 | empty |
| 3 | 131 | 0.71 | 0.92 | 28 | empty |
| 4 | 64 | 0.71 | 0.97 | 24 | empty |
| 5 | 150 | 0.70 | 0.90 | 37 | empty |
Interfaces
15 interfaces between chains.
- A–B · 2528 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 2516 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 2510 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 704 Ų buried · 10 hydrogen bonds · protein-protein
- C–E · 699 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2ZDS · Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2) · 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 O69946
- Elsewhere: RCSB PDB 2ZDS · PDBe 2ZDS · UniProt O69946
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