Research workbench
P-EIF2A - EIF2B complex
Analyse P-EIF2A - EIF2B complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JLZ
- Type
- protein
- Length
- 4,039 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor eif-2B subunit alpha; Probable translation initiation…
- UniProt
- Q9USP0, Q9UT76, P56288, Q09924, P56287, P20459
- Ligands
- PO4
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 10 distinct chains · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor eif-2B subunit alpha | protein | 317 | 46% helix, 12% strand | Q9USP0 |
| B | Translation initiation factor eif-2B subunit alpha | protein | 315 | 46% helix, 13% strand | Q9USP0 |
| C, D | Probable translation initiation factor eif-2B subunit beta | protein | 337 | 49% helix, 15% strand | Q9UT76 |
| E, F | Probable translation initiation factor eif-2B subunit gamma | protein | 409 | 20% helix, 27% strand | P56288 |
| G | Probable translation initiation factor eif-2B subunit delta | protein | 360 | 45% helix, 13% strand | Q09924 |
| H | Probable translation initiation factor eif-2B subunit delta | protein | 361 | 45% helix, 14% strand | Q09924 |
| I | Probable translation initiation factor eif-2B subunit epsilon | protein | 430 | 21% helix, 25% strand | P56287 |
| J | Probable translation initiation factor eif-2B subunit epsilon | protein | 428 | 20% helix, 26% strand | P56287 |
| L | Eukaryotic translation initiation factor 2 subunit alpha | protein | 167 | 36% helix, 22% strand | P20459 |
| M | Eukaryotic translation initiation factor 2 subunit alpha | protein | 169 | 33% helix, 20% strand | P20459 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 12 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1065 | 0.89 | 0.90 | 174 | empty |
| 2 | 426 | 0.81 | 0.89 | 69 | empty |
| 3 | 901 | 0.79 | 0.81 | 76 | empty |
| 4 | 255 | 0.77 | 0.91 | 50 | PO4 |
| 5 | 753 | 0.77 | 0.81 | 71 | empty |
Interfaces
30 interfaces between chains.
- A–B · 3248 Ų buried · 38 hydrogen bonds · protein-protein
- D–H · 2350 Ų buried · 22 hydrogen bonds · protein-protein
- C–G · 2301 Ų buried · 22 hydrogen bonds · protein-protein
- D–J · 1475 Ų buried · 13 hydrogen bonds · protein-protein
- C–I · 1463 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6JLZ · P-eIF2a - eIF2B complex · the same entry in another collection · chain M against M, TM-score 1.00
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 Q9USP0
- Every structure of UniProt Q9UT76
- Every structure of UniProt P56288
- Every structure of UniProt Q09924
- Every structure of UniProt P56287
- Every structure of UniProt P20459
- Elsewhere: RCSB PDB 6JLZ · PDBe 6JLZ · UniProt Q9USP0 · UniProt Q9UT76 · UniProt P56288 · UniProt Q09924 · UniProt P56287 · UniProt P20459
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