Research workbench
D-erythronate-4-phosphate dehydrogenase complexed with NAD
Analyse D-erythronate-4-phosphate dehydrogenase complexed with NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OET
- Type
- protein
- Length
- 2,987 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P60802
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 375 | — | P60802 |
| B | — | protein | 377 | — | P60802 |
| C | — | protein | 372 | — | P60802 |
| D | — | protein | 375 | — | P60802 |
| E | — | protein | 375 | — | P60802 |
| F | — | protein | 365 | — | P60802 |
| G | — | protein | 370 | — | P60802 |
| H | — | protein | 378 | — | P60802 |
Compared structures
- 3OET · D-Erythronate-4-Phosphate Dehydrogenase complexed with NAD · the same entry in another collection · chain H against H, TM-score 1.00
- P60802 · AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (P60802) · a predicted model of the same protein · chain F 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 P60802
- Elsewhere: RCSB PDB 3OET · PDBe 3OET · UniProt P60802
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