Research workbench
E. COLI beta sliding clamp, 148-153 ala mutant
Analyse E. COLI beta sliding clamp, 148-153 ala mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F1V
- Type
- protein
- Length
- 732 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
- Ligands
- CA, CL
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA polymerase III subunit beta (EC 2.7.7.7) | protein | 366 | 21% helix, 46% strand | P0A988 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.56 | 0.80 | 27 | empty |
| 2 | 199 | 0.45 | 0.74 | 31 | empty |
| 3 | 79 | 0.32 | 0.74 | 17 | CA |
| 4 | 56 | 0.28 | 0.74 | 17 | empty |
| 5 | 52 | 0.26 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1284 Ų buried · 28 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 P0A988
- Elsewhere: RCSB PDB 3F1V · PDBe 3F1V · UniProt P0A988
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.