Research workbench
The G157C mutation in the escherichia COLI sliding clamp specifically affects initiation of replication
Analyse The G157C mutation in the escherichia COLI sliding clamp specifically affects… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XUR
- Type
- protein
- Length
- 730 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase III subunit beta
- EC
- 2.7.7.7
- UniProt
- P0A988
- Pockets
- 5 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase III subunit beta (EC 2.7.7.7) | protein | 366 | 22% helix, 46% strand | P0A988 |
| B | DNA polymerase III subunit beta (EC 2.7.7.7) | protein | 364 | 23% helix, 45% strand | P0A988 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.32 | 0.75 | 14 | empty |
| 2 | 71 | 0.31 | 0.74 | 22 | empty |
| 3 | 62 | 0.29 | 0.74 | 20 | empty |
| 4 | 57 | 0.29 | 0.75 | 15 | empty |
| 5 | 57 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1368 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 2XUR · The G157C mutation in the Escherichia coli sliding clamp specifically affects initiation… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A988 · AlphaFold monomer V2.0 prediction for beta sliding clamp (P0A988) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P0A988
- Elsewhere: RCSB PDB 2XUR · PDBe 2XUR · UniProt P0A988
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