Research workbench
Crystal structure of a DNA polymerase III alpha-epsilon chimera
Analyse Crystal structure of a DNA polymerase III alpha-epsilon chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GX9
- Type
- protein
- Length
- 1,254 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03007, P10443
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 312 | — | P03007, P10443 |
| B | — | protein | 313 | — | P03007, P10443 |
| C | — | protein | 317 | — | P03007, P10443 |
Compared structures
- 4GX9 · Crystal structure of a DNA polymerase III alpha-epsilon chimera · the same entry in another collection · chain A against A, TM-score 1.00
- P10443 · AlphaFold monomer V2.0 prediction for DNA polymerase III subunit alpha (P10443) · a predicted model of the same protein · chain D against A, TM-score 0.84
- P03007 · AlphaFold monomer V2.0 prediction for DNA polymerase III subunit epsilon (P03007) · a predicted model of the same protein · chain D against A, TM-score 0.26
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 P03007
- Every structure of UniProt P10443
- Elsewhere: RCSB PDB 4GX9 · PDBe 4GX9 · UniProt P03007 · UniProt P10443
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