Research workbench
Elongation factor 3 in complex with ADP
Analyse Elongation factor 3 in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IW3
- Type
- protein
- Length
- 1,952 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 3A
- UniProt
- P16521
- Ligands
- ADP, SO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 3A | protein | 972 | 49% helix, 15% strand | P16521 |
| B | Elongation factor 3A | protein | 980 | 49% helix, 14% strand | P16521 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 13 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, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.84 | 0.86 | 104 | SO4 |
| 2 | 1163 | 0.82 | 0.83 | 109 | empty |
| 3 | 830 | 0.80 | 0.83 | 74 | empty |
| 4 | 772 | 0.80 | 0.83 | 89 | SO4 |
| 5 | 223 | 0.79 | 0.93 | 43 | ADP |
Interfaces
1 interface between chains.
- A–B · 3410 Ų buried · 39 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 modified (engineered).
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 P16521
- Elsewhere: RCSB PDB 2IW3 · PDBe 2IW3 · UniProt P16521
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