Research workbench
AlphaFold monomer V2.0 prediction for carbonic anhydrase (P53615)
Analyse AlphaFold monomer V2.0 prediction for carbonic anhydrase (P53615) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P53615
- Type
- protein
- Length
- 221 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Carbonic anhydrase
- UniProt
- P53615
Structure
1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase | protein | 221 | 48% helix, 16% strand | P53615 |
Compared structures
- 3EYX · Crystal structure of Carbonic Anhydrase Nce103 from Saccharomyces cerevisiae · an experimental structure of the same protein · chain A against B, TM-score 0.88
- 3EYX · Crystal structure of carbonic anhydrase NCE103 from saccharomyces cerevisiae · an experimental structure of the same protein · chain A against B, TM-score 0.88
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 P53615
- Elsewhere: UniProt P53615 · AlphaFold DB P53615
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