Research workbench
Crystal structure of human eRF1/eRF3 complex
Analyse Crystal structure of human eRF1/eRF3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E1Y
- Type
- protein
- Length
- 2,176 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.8
- Source
- Homo sapiens
- Molecule
- Eukaryotic peptide chain release factor subunit 1; Eukaryotic peptide chain release…
- UniProt
- P62495, P15170
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.68
Structure
x-ray diffraction · resolution 3.8 · 3 distinct chains · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Eukaryotic peptide chain release factor subunit 1 | protein | 380 | 38% helix, 21% strand | P62495 |
| C, D | Eukaryotic peptide chain release factor subunit 1 | protein | 318 | 36% helix, 15% strand | P62495 |
| E, F, G, H | Eukaryotic peptide chain release factor GTP-binding subunit ERF3A | protein | 195 | 2% helix, 44% strand | P15170 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.68 | 0.78 | 45 | ATP |
| 2 | 493 | 0.67 | 0.78 | 46 | ATP |
| 3 | 601 | 0.66 | 0.76 | 64 | empty |
| 4 | 434 | 0.62 | 0.76 | 40 | empty |
| 5 | 422 | 0.61 | 0.76 | 44 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1360 Ų buried · 23 hydrogen bonds · protein-protein
- F–G · 917 Ų buried · 4 hydrogen bonds · protein-protein
- E–H · 914 Ų buried · 4 hydrogen bonds · protein-protein
- D–H · 552 Ų buried · 5 hydrogen bonds · protein-protein
- C–G · 551 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P62495
- Every structure of UniProt P15170
- Elsewhere: RCSB PDB 3E1Y · PDBe 3E1Y · UniProt P62495 · UniProt P15170
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.