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The complex structure of D-mandelate dehydrogenase with NADH
Analyse The complex structure of D-mandelate dehydrogenase with NADH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WFJ
- Type
- protein
- Length
- 2,292 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E3USM3
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | E3USM3 |
| B | — | protein | 295 | — | E3USM3 |
| C | — | protein | 295 | — | E3USM3 |
| D | — | protein | 293 | — | E3USM3 |
| E | — | protein | 299 | — | E3USM3 |
| F | — | protein | 263 | — | E3USM3 |
| G | — | protein | 298 | — | E3USM3 |
| H | — | protein | 250 | — | E3USM3 |
Compared structures
- 3WFJ · The complex structure of D-mandelate dehydrogenase with NADH · 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 E3USM3
- Elsewhere: RCSB PDB 3WFJ · PDBe 3WFJ · UniProt E3USM3
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