Research workbench
Crystal structure of a replication fork DNA polymerase editing complex at 2.7 a resolution
Analyse Crystal structure of a replication fork DNA polymerase editing complex at 2.7 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CLQ
- Type
- protein + DNA
- Length
- 926 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q38087
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | dna | 11 | — | — |
| D | — | dna | 12 | — | — |
| A | — | protein | 903 | — | Q38087 |
Compared structures
- 1CLQ · Crystal structure of a replication fork DNA polymerase editing complex at 2.7 a resolution · the same entry in another collection · chain E against E, TM-score 1.00
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 Q38087
- Elsewhere: RCSB PDB 1CLQ · PDBe 1CLQ · UniProt Q38087
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