MolNFT v1 · #50406 · protein
AlphaFold monomer V2.0 prediction for C4 phosphoenolpyruvate carboxylase (P30694)
P30694: “AlphaFold monomer V2.0 prediction for C4 phosphoenolpyruvate carboxylase (P30694)”. MolNFT v1 #50406 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P30694
- Type
- protein
- Length
- 966 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x61E65F88ec27E6A5EcEACd71FeF1FE2264bb3e71
- UniProt
- P30694
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 966 | — | P30694 |
Compared structures
- 4BXH · Resolving the activation site of positive regulators in plant phosphoenolpyruvate… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 4BXC · Resolving the activation site of positive regulators in plant phosphoenolpyruvate… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 4BXC · Resolving the activation site of positive regulators in plant phosphoenolpyruvate… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 3ZGE · Greater efficiency of photosynthetic carbon fixation due to single amino acid substitution · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 3ZGE · Greater efficiency of photosynthetic carbon fixation due to single amino acid substitution · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 P30694
- Elsewhere: UniProt P30694 · AlphaFold DB P30694
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