MolNFT v1 · #11478 · protein
Crystal structure of sulfolobus solfataricus elongation factor 1 alpha in complex with GDP
1JNY · Elongation factor 1-alpha: “Crystal structure of sulfolobus solfataricus elongation factor 1 alpha in complex with GDP”. X-ray diffraction, 1 ligand (GDP), 6 pockets (best druggability 0.64). MolNFT v1 #11478 on GenesisL1: 3D…
- PDB
- 1JNY
- Type
- protein
- Length
- 827 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 1-alpha
- UniProt
- P35021
- Ligands
- GDP
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 1-alpha | protein | 415 | 23% helix, 35% strand | P35021 |
| B | Elongation factor 1-alpha | protein | 412 | 22% helix, 37% strand | P35021 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.64 | 0.80 | 34 | empty |
| 2 | 266 | 0.53 | 0.75 | 28 | empty |
| 3 | 150 | 0.49 | 0.78 | 31 | empty |
| 4 | 143 | 0.44 | 0.75 | 20 | empty |
| 5 | 61 | 0.36 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 359 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1JNY · Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP · 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 A 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 1JNY · PDBe 1JNY · UniProt P35021
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