Research workbench
Crystal structure of CFIM68 RRM/CFIM25/RNA complex
Analyse Crystal structure of CFIM68 RRM/CFIM25/RNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q2T
- Type
- protein + RNA
- Length
- 603 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43809, Q16630
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 205 | — | O43809 |
| B | — | protein | 203 | — | O43809 |
| C | — | protein | 93 | — | Q16630 |
| D | — | protein | 92 | — | Q16630 |
| E, F | — | rna | 5 | — | — |
Compared structures
- 3Q2T · Crystal Structure of CFIm68 RRM/CFIm25/RNA complex · the same entry in another collection · chain F against F, 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 0.97
- 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 3Q2T · PDBe 3Q2T · UniProt O43809 · UniProt Q16630
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