Research workbench
Double complex of the tyrosine sensitive dahp synthase from S. cerevisiae with CO2+, pep and the E4P analogoue G3P
Analyse Double complex of the tyrosine sensitive dahp synthase from S. cerevisiae with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OF8
- Type
- protein
- Length
- 683 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32449
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 339 | — | P32449 |
| B | — | protein | 344 | — | P32449 |
Compared structures
- 1OF8 · double complex of the tyrosine sensitive DAHP Synthase from S. cerevisiae with Co2+, PEP… · the same entry in another collection · chain A against A, TM-score 1.00
- P32449 · AlphaFold monomer V2.0 prediction for phospho-2-dehydro-3-deoxyheptonate aldolase… · a predicted model of the same protein · chain A 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 P32449
- Elsewhere: RCSB PDB 1OF8 · PDBe 1OF8 · UniProt P32449
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