MolNFT v1 · #12540 · protein
Structure of the large gamma subunit of initiation factor EIF2 from pyrococcus abyssi-G235D mutant
1KJZ · EIF2GAMMA: “Structure of the large gamma subunit of initiation factor EIF2 from pyrococcus abyssi-G235D mutant”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.57). MolNFT v1 #12540 on GenesisL1: 3D structure…
- PDB
- 1KJZ
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EIF2GAMMA
- UniProt
- Q9V1G0
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | EIF2GAMMA | protein | 400 | 19% helix, 41% strand | Q9V1G0 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.57 | 0.76 | 43 | empty |
| 2 | 166 | 0.55 | 0.80 | 36 | empty |
| 3 | 118 | 0.43 | 0.77 | 21 | empty |
| 4 | 89 | 0.42 | 0.79 | 15 | empty |
| 5 | 80 | 0.34 | 0.75 | 15 | empty |
Compared structures
- 1KJZ · Structure of the large gamma subunit of initiation factor eIF2 from Pyrococcus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9V1G0 · AlphaFold monomer V2.0 prediction for translation initiation factor 2 subunit gamma… · a predicted model of the same protein · chain A against A, TM-score 0.88
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 Q9V1G0
- Elsewhere: RCSB PDB 1KJZ · PDBe 1KJZ · UniProt Q9V1G0
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