Research workbench
Structural study of project id PH0725 from pyrococcus horikoshii OT3 (K19M)
Analyse Structural study of project id PH0725 from pyrococcus horikoshii OT3 (K19M) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E8Q
- Type
- protein
- Length
- 530 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable diphthine synthase
- EC
- 2.1.1.98
- UniProt
- O58456
- Ligands
- SAH
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable diphthine synthase (EC 2.1.1.98) | protein | 265 | 36% helix, 22% strand | O58456 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.76 | 0.83 | 52 | empty |
| 2 | 432 | 0.73 | 0.83 | 60 | SAH |
| 3 | 153 | 0.44 | 0.75 | 22 | empty |
| 4 | 101 | 0.41 | 0.77 | 20 | empty |
| 5 | 90 | 0.41 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2428 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2E8Q · Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M) · the same entry in another collection · chain A against A, TM-score 1.00
- O58456 · AlphaFold monomer V2.0 prediction for diphthine synthase (O58456) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O58456
- Elsewhere: RCSB PDB 2E8Q · PDBe 2E8Q · UniProt O58456
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