Research workbench
Structure of transhydrogenase (DI.NAD+)2(DIII.H2NADPH)1 asymmetric complex
Analyse Structure of transhydrogenase (DI.NAD+)2(DIII.H2NADPH)1 asymmetric complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OOR
- Type
- protein
- Length
- 915 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD(P) transhydrogenase subunit alpha part 1; NAD(P) transhydrogenase subunit beta
- EC
- 1.6.1.2
- UniProt
- P0C186, P0C188
- Ligands
- NAD, TXP
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P) transhydrogenase subunit alpha part 1 (EC 1.6.1.2) | protein | 378 | 36% helix, 18% strand | P0C186 |
| B | NAD(P) transhydrogenase subunit alpha part 1 (EC 1.6.1.2) | protein | 364 | 38% helix, 20% strand | P0C186 |
| C | NAD(P) transhydrogenase subunit beta (EC 1.6.1.2) | protein | 173 | 42% helix, 19% strand | P0C188 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B, C
- TXP · 1,4,5,6-tetrahydronicotinamide adenine dinucleotide phosphate · ligand · chains B, C
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1013 | 0.80 | 0.82 | 111 | NAD, GOL, TXP |
| 2 | 974 | 0.77 | 0.79 | 78 | NAD |
| 3 | 361 | 0.60 | 0.76 | 53 | empty |
| 4 | 155 | 0.46 | 0.76 | 24 | empty |
| 5 | 164 | 0.43 | 0.74 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1788 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 728 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 413 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2OOR · Structure of transhydrogenase (dI.NAD+)2(dIII.H2NADPH)1 asymmetric complex · the same entry in another collection · chain A against A, TM-score 1.00
- P0C186 · AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase subunit alpha part 1… · a predicted model of the same protein · chain A against A, TM-score 0.99
- P0C188 · AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase subunit beta (P0C188) · a predicted model of the same protein · chain C 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 P0C186
- Every structure of UniProt P0C188
- Elsewhere: RCSB PDB 2OOR · PDBe 2OOR · UniProt P0C186 · UniProt P0C188
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