MolNFT v1 · #116858 · protein
Complex structure of human elongation factor 1B alpha and gamma GST- like domains
5DQS · Elongation factor 1-gamma: “Complex structure of human elongation factor 1B alpha and gamma GST- like domains”. X-ray diffraction, 2 pockets (best druggability 0.39). MolNFT v1 #116858 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5DQS
- Type
- protein
- Length
- 297 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 1-gamma; Elongation factor 1-beta
- UniProt
- P26641, P24534
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 1-gamma | protein | 210 | 58% helix, 8% strand | P26641 |
| D | Elongation factor 1-beta | protein | 87 | 43% helix, 0% strand | P24534 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.39 | 0.78 | 14 | empty |
| 2 | 110 | 0.37 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–D · 632 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 5DQS · Complex structure of human elongation factor 1B alpha and gamma GST-like domains · the same entry in another collection · chain A against A, TM-score 1.00
- P26641 · AlphaFold monomer V2.0 prediction for elongation factor 1-gamma (P26641) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P24534 · AlphaFold monomer V2.0 prediction for elongation factor 1-beta (P24534) · a predicted model of the same protein · chain D against A, TM-score 0.93
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 P26641
- Every structure of UniProt P24534
- Elsewhere: RCSB PDB 5DQS · PDBe 5DQS · UniProt P26641 · UniProt P24534
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