Research workbench
Crystal structure of CFIM68 RRM/CFIM25 complex
Analyse Crystal structure of CFIM68 RRM/CFIM25 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q2S
- Type
- protein
- Length
- 595 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cleavage and polyadenylation specificity factor subunit 5; Cleavage and polyadenylation…
- UniProt
- O43809, Q16630
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cleavage and polyadenylation specificity factor subunit 5 | protein | 207 | 22% helix, 36% strand | O43809 |
| B | Cleavage and polyadenylation specificity factor subunit 5 | protein | 203 | 21% helix, 33% strand | O43809 |
| C | Cleavage and polyadenylation specificity factor subunit 6 | protein | 93 | 27% helix, 30% strand | Q16630 |
| D | Cleavage and polyadenylation specificity factor subunit 6 | protein | 92 | 26% helix, 26% strand | Q16630 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 604 | 0.71 | 0.79 | 60 | empty |
| 2 | 454 | 0.67 | 0.79 | 52 | empty |
| 3 | 203 | 0.52 | 0.77 | 29 | empty |
| 4 | 151 | 0.51 | 0.79 | 30 | empty |
| 5 | 119 | 0.49 | 0.80 | 21 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1471 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 596 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 511 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 278 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 269 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3Q2S · Crystal Structure of CFIm68 RRM/CFIm25 complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q16630 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain C against A, TM-score 0.98
- O43809 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain B against A, TM-score 0.96
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 O43809
- Every structure of UniProt Q16630
- Elsewhere: RCSB PDB 3Q2S · PDBe 3Q2S · UniProt O43809 · UniProt Q16630
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