MolNFT v1 · #16010 · protein
R. rubrum transhydrogenase (DI.Q132N)2(DIII)1 asymmetric complex
1NM5: “R. rubrum transhydrogenase (DI.Q132N)2(DIII)1 asymmetric complex”. X-ray diffraction. MolNFT v1 #16010 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NM5
- Type
- protein
- Length
- 892 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q60164, Q59765
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 360 | — | Q60164 |
| B | — | protein | 358 | — | Q60164 |
| C | — | protein | 174 | — | Q59765 |
Compared structures
- 1NM5 · R. rubrum transhydrogenase (dI.Q132N)2(dIII)1 asymmetric complex · 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 Q60164
- Every structure of UniProt Q59765
- Elsewhere: RCSB PDB 1NM5 · PDBe 1NM5 · UniProt Q60164 · UniProt Q59765
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