Research workbench
A conserved protein binding-site on bacterial sliding clamps
Analyse A conserved protein binding-site on bacterial sliding clamps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OK7
- Type
- protein
- Length
- 739 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase III; DNA polymerase IV
- EC
- 2.7.7.7
- UniProt
- P00583, Q47155
- Pockets
- 3 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA polymerase III (EC 2.7.7.7) | protein | 366 | 22% helix, 47% strand | P00583 |
| C | DNA polymerase IV (EC 2.7.7.7) | protein | 7 | 0% helix, 14% strand | Q47155 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.38 | 0.74 | 22 | empty |
| 2 | 75 | 0.32 | 0.74 | 20 | empty |
| 3 | 56 | 0.25 | 0.72 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1269 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 602 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 P00583
- Every structure of UniProt Q47155
- Elsewhere: RCSB PDB 1OK7 · PDBe 1OK7 · UniProt P00583 · UniProt Q47155
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