Research workbench
The asymmetric complex of the two nucleotide-binding components (di, diii) of proton-translocating transhydrogenase
Analyse The asymmetric complex of the two nucleotide-binding components (di, diii) of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HZZ
- Type
- protein
- Length
- 902 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 | 362 | — | Q60164 |
| B | — | protein | 366 | — | Q60164 |
| C | — | protein | 174 | — | Q59765 |
Compared structures
- 1HZZ · The asymmetric complex of the two nucleotide-binding components (di, diii) of… · 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 1HZZ · PDBe 1HZZ · UniProt Q60164 · UniProt Q59765
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