Research workbench
Crystal structure of the complex between human fmrp rgg motif and G- quadruplex RNA, iridium hexammine bound form.
Analyse Crystal structure of the complex between human fmrp rgg motif and G- quadruplex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DE8
- Type
- protein + RNA
- Length
- 98 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SC1; Fragile X mental retardation protein 1
- UniProt
- Q06787
- Ligands
- IRI, K
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | SC1 | rna | 35 | — | — |
| B | Fragile X mental retardation protein 1 | protein | 14 | 0% helix, 0% strand | Q06787 |
| D | Fragile X mental retardation protein 1 | protein | 14 | 0% helix, 0% strand | Q06787 |
Ligands and binding sites
- IRI · Iridium hexammine ion · ligand · 5 copies · chains A, C
- K · Potassium ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- A–B · 688 Ų buried · 33 hydrogen bonds · protein-nucleic
- C–D · 646 Ų buried · 31 hydrogen bonds · protein-nucleic
- A–C · 195 Ų buried · 7 hydrogen bonds · nucleic-nucleic
- B–C · 46 Ų buried · 0 hydrogen bonds · protein-nucleic
- A–D · 26 Ų buried · 0 hydrogen bonds · protein-nucleic
Compared structures
- 5DE8 · Crystal structure of the complex between human FMRP RGG motif and G-quadruplex RNA… · the same entry in another collection · chain A against A, TM-score 1.00
- Q06787 · AlphaFold monomer V2.0 prediction for synaptic functional regulator FMR1 (Q06787) · a predicted model of the same protein · chain D against A, TM-score 0.26
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 Q06787
- Elsewhere: RCSB PDB 5DE8 · PDBe 5DE8 · UniProt Q06787
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