Research workbench
AlphaFold monomer V2.0 prediction for dihydrofolate reductase hdra (P15093)
Analyse AlphaFold monomer V2.0 prediction for dihydrofolate reductase hdra (P15093) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P15093
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- UniProt
- P15093
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 162 | — | P15093 |
Compared structures
- 1VDR · Dihydrofolate reductase · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 1VDR · Dihydrofolate reductase · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 2JYB · Binary HVDHFR1:FOLATE complex · an experimental structure of the same protein · chain A against A, TM-score 0.88
- 2JYB · binary hvDHFR1:folate complex · an experimental structure of the same protein · chain A against A, TM-score 0.88
- 2ITH · NMR Structure of Haloferax volcanii DHFR · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 2ITH · NMR structure of haloferax volcanii DHFR · an experimental structure of the same protein · chain A against A, TM-score 0.86
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 P15093
- Elsewhere: UniProt P15093 · AlphaFold DB P15093
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