Research workbench
AlphaFold monomer V2.0 prediction for chlorophyll a-B binding protein CP29 (Q93WD2)
Analyse AlphaFold monomer V2.0 prediction for chlorophyll a-B binding protein CP29… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q93WD2
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0e1cf82d2E07cf9FCd6ce0e123Bc9584e4F92CaD
- UniProt
- Q93WD2
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 280 | — | Q93WD2 |
Compared structures
- 6KAD · Cryo-EM structure of the C2S2M2L2-type PSII-LHCII supercomplex from Chlamydomonas… · an experimental structure of the same protein · chain A against r, TM-score 0.81
- 6KAF · C2S2M2N2-type PSII-LHCII · an experimental structure of the same protein · chain A against R, TM-score 0.75
- 6KAC · Cryo-EM structure of the C2S2-type psii-lhcii supercomplex from chlamydomonas reihardtii · an experimental structure of the same protein · chain A against R, TM-score 0.62
- 6KAC · Cryo-EM structure of the C2S2-type PSII-LHCII supercomplex from Chlamydomonas reihardtii · an experimental structure of the same protein · chain A against R, TM-score 0.62
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 Q93WD2
- Elsewhere: UniProt Q93WD2 · AlphaFold DB Q93WD2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.