MolNFT v1 · #47109 · protein
Structure of transhydrogenase (DI.NAD+)2(DIII.H2NADPH)1 asymmetric complex
2OOR: “Structure of transhydrogenase (DI.NAD+)2(DIII.H2NADPH)1 asymmetric complex”. X-ray diffraction. MolNFT v1 #47109 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2OOR
- Type
- protein
- Length
- 915 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0C186, P0C188
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 378 | — | P0C186 |
| B | — | protein | 364 | — | P0C186 |
| C | — | protein | 173 | — | P0C188 |
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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