Research workbench
Nucleotide-free form of an isolated E. COLI clamp loader gamma subunit
Analyse Nucleotide-free form of an isolated E. COLI clamp loader gamma subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NJG
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA polymerase III subunit gamma
- EC
- 2.7.7.7
- UniProt
- P06710
- Ligands
- ZN, SO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA polymerase III subunit gamma (EC 2.7.7.7) | protein | 240 | 49% helix, 12% strand | P06710 |
| B | DNA polymerase III subunit gamma (EC 2.7.7.7) | protein | 239 | 49% helix, 12% strand | P06710 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.65 | 0.86 | 27 | empty |
| 2 | 107 | 0.64 | 0.88 | 23 | empty |
| 3 | 422 | 0.61 | 0.77 | 45 | SO4 |
| 4 | 229 | 0.54 | 0.77 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1NJG · Nucleotide-free form of an Isolated E. coli Clamp Loader Gamma Subunit · the same entry in another collection · chain A against A, TM-score 1.00
- P06710 · AlphaFold monomer V2.0 prediction for DNA polymerase III subunit tau (P06710) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P06710
- Elsewhere: RCSB PDB 1NJG · PDBe 1NJG · UniProt P06710
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