Research workbench
Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor ire B RNA
Analyse Crystal structure analysis of iron regulatory protein 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SN2
- Type
- protein + RNA
- Length
- 877 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic aconitate hydratase; Transferrin receptor iron regulatory element B RNA
- EC
- 4.2.1.3
- UniProt
- Q01059
- Pockets
- 11 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic aconitate hydratase (EC 4.2.1.3) | protein | 848 | 38% helix, 20% strand | Q01059 |
| B | Transferrin receptor iron regulatory element B RNA | rna | 29 | — | — |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.74 | 0.83 | 61 | empty |
| 2 | 337 | 0.73 | 0.85 | 44 | empty |
| 3 | 811 | 0.66 | 0.74 | 63 | empty |
| 4 | 198 | 0.63 | 0.84 | 36 | empty |
| 5 | 227 | 0.61 | 0.81 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 1477 Ų buried · 40 hydrogen bonds · protein-nucleic
Compared structures
- 3SN2 · Crystal structure analysis of iron regulatory protein 1 in complex with transferrin… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01059 · AlphaFold monomer V2.0 prediction for cytoplasmic aconitate hydratase (Q01059) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 Q01059
- Elsewhere: RCSB PDB 3SN2 · PDBe 3SN2 · UniProt Q01059
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