Research workbench
Structure of EIF2B-EIF2 (phosphorylated at SER51) complex (model C)
Analyse Structure of EIF2B-EIF2 (phosphorylated at SER51) complex (model C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QG5
- Type
- protein
- Length
- 4,853 residues
- Chains
- 16
- 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
- P14741, P32502, P09032, P12754, P32501, P20459, P32481, P09064
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 9 distinct chains · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Translation initiation factor eif-2B subunit alpha | protein | 302 | 39% helix, 12% strand | P14741 |
| C, D | Translation initiation factor eif-2B subunit beta | protein | 345 | 45% helix, 13% strand | P32502 |
| E, F | Translation initiation factor eif-2B subunit gamma | protein | 267 | 19% helix, 18% strand | P09032 |
| G, H | Translation initiation factor eif-2B subunit delta | protein | 355 | 38% helix, 12% strand | P12754 |
| I, J | Translation initiation factor eif-2B subunit epsilon | protein | 431 | 19% helix, 24% strand | P32501 |
| K, L | Eukaryotic translation initiation factor 2 subunit alpha | protein | 246 | 34% helix, 21% strand | P20459 |
| M, N | Eukaryotic translation initiation factor 2 subunit gamma | protein | 408 | 13% helix, 37% strand | P32481 |
| O | Eukaryotic translation initiation factor 2 subunit beta | protein | 17 | 65% helix, 0% strand | P09064 |
| P | Eukaryotic translation initiation factor 2 subunit beta | protein | 128 | 27% helix, 18% strand | P09064 |
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 | 586 | 0.87 | 0.93 | 95 | empty |
| 2 | 378 | 0.84 | 0.93 | 57 | empty |
| 3 | 1146 | 0.84 | 0.85 | 117 | empty |
| 4 | 1051 | 0.84 | 0.85 | 90 | empty |
| 5 | 920 | 0.82 | 0.84 | 107 | empty |
Interfaces
36 interfaces between chains.
- C–G · 2616 Ų buried · 16 hydrogen bonds · protein-protein
- D–H · 2375 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 2211 Ų buried · 33 hydrogen bonds · protein-protein
- D–J · 1364 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1358 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6QG5 · Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (model C) · the same entry in another collection · chain K against K, 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 P14741
- Every structure of UniProt P32502
- Every structure of UniProt P09032
- Every structure of UniProt P12754
- Every structure of UniProt P32501
- Every structure of UniProt P20459
- Every structure of UniProt P32481
- Every structure of UniProt P09064
- Elsewhere: RCSB PDB 6QG5 · PDBe 6QG5 · UniProt P14741 · UniProt P32502 · UniProt P09032 · UniProt P12754 · UniProt P32501 · UniProt P20459 · UniProt P32481 · UniProt P09064
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