Research workbench
Crystal structure of IMP3 RRM12 in complex with RNA (cccc)
Analyse Crystal structure of IMP3 RRM12 in complex with RNA (cccc) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FQR
- Type
- protein + RNA
- Length
- 321 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like growth factor 2 mRNA-binding protein 3; RNA cccc
- UniProt
- O00425
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like growth factor 2 mRNA-binding protein 3 | protein | 158 | 27% helix, 30% strand | O00425 |
| B | Insulin-like growth factor 2 mRNA-binding protein 3 | protein | 160 | 27% helix, 30% strand | O00425 |
| C | RNA cccc | rna | 3 | — | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.48 | 0.78 | 21 | empty |
| 2 | 67 | 0.34 | 0.76 | 15 | empty |
| 3 | 54 | 0.27 | 0.75 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 460 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 389 Ų buried · 7 hydrogen bonds · protein-nucleic
- B–C · 86 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 6FQR · Crystal structure of IMP3 RRM12 in complex with RNA (CCCC) · the same entry in another collection · chain A against A, TM-score 1.00
- O00425 · AlphaFold monomer V2.0 prediction for insulin-like growth factor 2 mRNA-binding protein 3… · a predicted model of the same protein · chain A against A, TM-score 0.54
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 O00425
- Elsewhere: RCSB PDB 6FQR · PDBe 6FQR · UniProt O00425
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