Research workbench
Crystal structure of the RAD4-RAD23 complex
Analyse Crystal structure of the RAD4-RAD23 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QSF
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein RAD4; UV excision repair protein RAD23
- UniProt
- P14736, P32628
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein RAD4 | protein | 486 | 38% helix, 20% strand | P14736 |
| X | UV excision repair protein RAD23 | protein | 104 | 69% helix, 2% strand | P32628 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.64 | 0.81 | 41 | empty |
| 2 | 248 | 0.64 | 0.82 | 34 | empty |
| 3 | 216 | 0.51 | 0.76 | 24 | empty |
| 4 | 120 | 0.47 | 0.78 | 15 | empty |
| 5 | 65 | 0.36 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–X · 1803 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2QSF · Crystal structure of the Rad4-Rad23 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P14736 · AlphaFold monomer V2.0 prediction for DNA repair protein RAD4 (P14736) · a predicted model of the same protein · chain A against A, TM-score 0.93
- P32628 · AlphaFold monomer V2.0 prediction for UV excision repair protein RAD23 (P32628) · a predicted model of the same protein · chain X against A, TM-score 0.52
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 P14736
- Every structure of UniProt P32628
- Elsewhere: RCSB PDB 2QSF · PDBe 2QSF · UniProt P14736 · UniProt P32628
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