MolNFT v1 · #21763 · protein
The crystal structure of sulfolobus solfataricus elongation factor 1- alpha in complex with magnesium and GDP
1SKQ · Elongation factor 1-alpha: “The crystal structure of sulfolobus solfataricus elongation factor 1- alpha in complex with magnesium and GDP”. X-ray diffraction, 2 ligands (GDP, MG), 8 pockets (best druggability 0.62). MolNFT v1 #21763…
- PDB
- 1SKQ
- Type
- protein
- Length
- 832 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 1-alpha
- UniProt
- P35021
- Ligands
- GDP, MG
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Elongation factor 1-alpha | protein | 416 | 23% helix, 35% strand | P35021 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.62 | 0.80 | 45 | empty |
| 2 | 244 | 0.51 | 0.75 | 29 | empty |
| 3 | 129 | 0.46 | 0.78 | 22 | empty |
| 4 | 153 | 0.46 | 0.76 | 27 | MG |
| 5 | 128 | 0.38 | 0.73 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 361 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1SKQ · The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P35021 · AlphaFold monomer V2.0 prediction for elongation factor 1-alpha (P35021) · a predicted model of the same protein · chain B against A, TM-score 0.54
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 P35021
- Elsewhere: RCSB PDB 1SKQ · PDBe 1SKQ · UniProt P35021
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