Research workbench
Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer
Analyse Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O93
- Type
- protein
- Length
- 708 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.77
- Source
- Thermus thermophilus
- Molecule
- NAD(P) transhydrogenase subunit alpha 2; NAD(P) transhydrogenase subunit beta
- EC
- 1.6.1.2
- UniProt
- Q72GR9, Q72GS0
- Ligands
- HG
- Pockets
- 9 · best druggability 0.56
Structure
x-ray diffraction · resolution 2.77 · 4 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P) transhydrogenase subunit alpha 2 (EC 1.6.1.2) | protein | 94 | 79% helix, 0% strand | Q72GR9 |
| B | NAD(P) transhydrogenase subunit beta (EC 1.6.1.2) | protein | 264 | 79% helix, 0% strand | Q72GS0 |
| C | NAD(P) transhydrogenase subunit alpha 2 (EC 1.6.1.2) | protein | 90 | 79% helix, 0% strand | Q72GR9 |
| D | NAD(P) transhydrogenase subunit beta (EC 1.6.1.2) | protein | 260 | 79% helix, 0% strand | Q72GS0 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.56 | 0.79 | 36 | empty |
| 2 | 230 | 0.54 | 0.77 | 34 | empty |
| 3 | 135 | 0.45 | 0.76 | 19 | empty |
| 4 | 129 | 0.45 | 0.76 | 19 | empty |
| 5 | 149 | 0.44 | 0.75 | 16 | empty |
Interfaces
5 interfaces between chains.
- C–D · 3636 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 3548 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 584 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 487 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 484 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4O93 · Crystal structure of thermus thermophilis transhydrogeanse domain II dimer · the same entry in another collection · chain A against A, 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 Q72GR9
- Every structure of UniProt Q72GS0
- Elsewhere: RCSB PDB 4O93 · PDBe 4O93 · UniProt Q72GR9 · UniProt Q72GS0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.