Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine reductase (B4S5H3)
Analyse AlphaFold monomer V2.0 prediction for NADPH-dependent 7-cyano-7-deazaguanine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4S5H3
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- UniProt
- B4S5H3
Structure
1 distinct chain · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent 7-cyano-7-deazaguanine reductase | protein | 118 | 27% helix, 39% strand | B4S5H3 |
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 B4S5H3
- Elsewhere: UniProt B4S5H3 · AlphaFold DB B4S5H3
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