Research workbench
Crystal structure analysis of the translation factor RF3
Analyse Crystal structure analysis of the translation factor RF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VR1
- Type
- protein
- Length
- 2,064 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide chain release factor 3
- UniProt
- B8DIL5
- Ligands
- G4P
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Peptide chain release factor 3 | protein | 516 | 34% helix, 28% strand | B8DIL5 |
Ligands and binding sites
- G4P · Guanosine-5',3'-tetraphosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.80 | 0.82 | 122 | empty |
| 2 | 1072 | 0.79 | 0.81 | 107 | G4P |
| 3 | 586 | 0.78 | 0.84 | 64 | G4P |
| 4 | 672 | 0.77 | 0.83 | 63 | G4P |
| 5 | 628 | 0.76 | 0.82 | 62 | G4P |
Interfaces
4 interfaces between chains.
- A–C · 1041 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1023 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 985 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 737 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 B8DIL5
- Elsewhere: RCSB PDB 3VR1 · PDBe 3VR1 · UniProt B8DIL5
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