Research workbench
Structure of the human DDB1-csa complex
Analyse Structure of the human DDB1-csa complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FCV
- Type
- protein
- Length
- 1,456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16531, Q13216
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1091 | — | Q16531 |
| B | — | protein | 365 | — | Q13216 |
Compared structures
- 6FCV · Structure of the human DDB1-CSA complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q13216 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-8 (Q13216) · a predicted model of the same protein · chain B against A, TM-score 1.00
- Q16531 · AlphaFold monomer V2.0 prediction for DNA damage-binding protein 1 (Q16531) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 Q16531
- Every structure of UniProt Q13216
- Elsewhere: RCSB PDB 6FCV · PDBe 6FCV · UniProt Q16531 · UniProt Q13216
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