Research workbench
EIF2B-EIF2(AP), AP2 complex
Analyse EIF2B-EIF2(AP), AP2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D44
- Type
- protein
- Length
- 3,825 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor eif-2B subunit alpha; Translation initiation factor eif-2B…
- UniProt
- Q14232, P49770, Q9NR50, Q9UI10, Q13144, P05198
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 9 distinct chains · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor eif-2B subunit alpha | protein | 293 | 46% helix, 13% strand | Q14232 |
| B | Translation initiation factor eif-2B subunit alpha | protein | 291 | 46% helix, 13% strand | Q14232 |
| C | Translation initiation factor eif-2B subunit beta | protein | 317 | 50% helix, 14% strand | P49770 |
| D | Translation initiation factor eif-2B subunit beta | protein | 324 | 48% helix, 12% strand | P49770 |
| E, F | Translation initiation factor eif-2B subunit gamma | protein | 343 | 20% helix, 18% strand | Q9NR50 |
| G, H | Translation initiation factor eif-2B subunit delta | protein | 353 | 42% helix, 10% strand | Q9UI10 |
| I | Translation initiation factor eif-2B subunit epsilon | protein | 427 | 21% helix, 18% strand | Q13144 |
| J | Translation initiation factor eif-2B subunit epsilon | protein | 429 | 21% helix, 17% strand | Q13144 |
| K, L | Eukaryotic translation initiation factor 2 subunit 1 | protein | 176 | 40% helix, 16% strand | P05198 |
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 | 1117 | 0.86 | 0.87 | 131 | empty |
| 2 | 699 | 0.83 | 0.87 | 68 | empty |
| 3 | 714 | 0.82 | 0.86 | 75 | empty |
| 4 | 509 | 0.80 | 0.87 | 69 | empty |
| 5 | 541 | 0.79 | 0.86 | 44 | empty |
Interfaces
26 interfaces between chains.
- C–G · 2220 Ų buried · 18 hydrogen bonds · protein-protein
- D–H · 2142 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1375 Ų buried · 19 hydrogen bonds · protein-protein
- D–J · 1319 Ų buried · 10 hydrogen bonds · protein-protein
- C–I · 1280 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 7D44 · eIF2B-eIF2(aP), aP2 complex · the same entry in another collection · chain L against L, 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 Q14232
- Every structure of UniProt P49770
- Every structure of UniProt Q9NR50
- Every structure of UniProt Q9UI10
- Every structure of UniProt Q13144
- Every structure of UniProt P05198
- Elsewhere: RCSB PDB 7D44 · PDBe 7D44 · UniProt Q14232 · UniProt P49770 · UniProt Q9NR50 · UniProt Q9UI10 · UniProt Q13144 · UniProt P05198
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