Research workbench
Crystal structure of the eukaryotic initiation factor 2B from leishmania major at 2.1 a resolution
Analyse Crystal structure of the eukaryotic initiation factor 2B from leishmania major… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A0U
- Type
- protein
- Length
- 741 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Initiation factor 2B
- UniProt
- Q4Q0R9
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Initiation factor 2B | protein | 374 | 43% helix, 16% strand | Q4Q0R9 |
| B | Initiation factor 2B | protein | 367 | 44% helix, 17% strand | Q4Q0R9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.76 | 0.99 | 33 | SO4 |
| 2 | 358 | 0.73 | 0.85 | 50 | empty |
| 3 | 64 | 0.73 | 0.98 | 26 | SO4 |
| 4 | 135 | 0.48 | 0.78 | 23 | empty |
| 5 | 138 | 0.46 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2374 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 2A0U · Crystal structure of the eukaryotic initiation factor 2B from Leishmania major at 2.1 A… · the same entry in another collection · chain A against A, TM-score 1.00
- Q4Q0R9 · AlphaFold monomer V2.0 prediction for methylthioribose-1-phosphate isomerase (Q4Q0R9) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q4Q0R9
- Elsewhere: RCSB PDB 2A0U · PDBe 2A0U · UniProt Q4Q0R9
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