Research workbench
Crystal structure of the human CPSF160-WDR33 complex
Analyse Crystal structure of the human CPSF160-WDR33 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F9N
- Type
- protein
- Length
- 1,537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cleavage and polyadenylation specificity factor subunit 1; Pre-mRNA 3' end processing…
- UniProt
- Q10570, Q9C0J8
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cleavage and polyadenylation specificity factor subunit 1 | protein | 1180 | 6% helix, 49% strand | Q10570 |
| B | Pre-mRNA 3' end processing protein WDR33 | protein | 357 | 6% helix, 43% strand | Q9C0J8 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 864 | 0.88 | 0.90 | 106 | empty |
| 2 | 1052 | 0.87 | 0.88 | 103 | empty |
| 3 | 910 | 0.81 | 0.83 | 69 | empty |
| 4 | 401 | 0.81 | 0.90 | 36 | empty |
| 5 | 584 | 0.78 | 0.83 | 48 | empty |
Interfaces
1 interface between chains.
- A–B · 3618 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 6F9N · Crystal structure of the human CPSF160-WDR33 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C0J8 · AlphaFold monomer V2.0 prediction for pre-mRNA 3' end processing protein WDR33 (Q9C0J8) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q10570 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q10570
- Every structure of UniProt Q9C0J8
- Elsewhere: RCSB PDB 6F9N · PDBe 6F9N · UniProt Q10570 · UniProt Q9C0J8
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