Research workbench
Crystal structure of the elongator subcomplex ELP456
Analyse Crystal structure of the elongator subcomplex ELP456 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A8J
- Type
- protein
- Length
- 1,523 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongator complex protein 4; Elongator complex protein 5; Elongator complex protein 6
- UniProt
- Q02884, P38874, Q04868
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 6 distinct chains · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongator complex protein 4 | protein | 277 | 33% helix, 26% strand | Q02884 |
| B | Elongator complex protein 5 | protein | 220 | 29% helix, 27% strand | P38874 |
| C | Elongator complex protein 6 | protein | 263 | 37% helix, 23% strand | Q04868 |
| D | Elongator complex protein 4 | protein | 280 | 32% helix, 25% strand | Q02884 |
| E | Elongator complex protein 5 | protein | 221 | 29% helix, 27% strand | P38874 |
| F | Elongator complex protein 6 | protein | 262 | 35% helix, 23% strand | Q04868 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 412 | 0.73 | 0.83 | 52 | empty |
| 2 | 424 | 0.72 | 0.83 | 54 | empty |
| 3 | 397 | 0.68 | 0.80 | 41 | empty |
| 4 | 381 | 0.68 | 0.81 | 32 | empty |
| 5 | 383 | 0.62 | 0.77 | 39 | empty |
Interfaces
8 interfaces between chains.
- C–E · 1660 Ų buried · 20 hydrogen bonds · protein-protein
- B–F · 1651 Ų buried · 22 hydrogen bonds · protein-protein
- D–F · 1406 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 1403 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 912 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 4A8J · Crystal Structure of the Elongator subcomplex Elp456 · the same entry in another collection · chain F against F, TM-score 1.00
- Q02884 · AlphaFold monomer V2.0 prediction for elongator complex protein 4 (Q02884) · a predicted model of the same protein · chain D against A, TM-score 1.00
- P38874 · AlphaFold monomer V2.0 prediction for elongator complex protein 5 (P38874) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q04868 · AlphaFold monomer V2.0 prediction for elongator complex protein 6 (Q04868) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 Q02884
- Every structure of UniProt P38874
- Every structure of UniProt Q04868
- Elsewhere: RCSB PDB 4A8J · PDBe 4A8J · UniProt Q02884 · UniProt P38874 · UniProt Q04868
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.