Research workbench
AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase ADENYLYLTRANSFERASE/ADENYLYL-removing enzyme (P30870)
Analyse AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P30870
- Type
- protein
- Length
- 946 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- UniProt
- P30870
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 946 | — | P30870 |
Compared structures
- 3K7D · C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 3K7D · C-terminal (adenylylation) domain of E.COLI glutamine synthetase adenylyltransferase · an experimental structure of the same protein · chain A against A, TM-score 0.52
- 1V4A · Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase… · an experimental structure of the same protein · chain A against A, TM-score 0.45
- 1V4A · Structure of the N-terminal domain of escherichia COLI glutamine synthetase… · an experimental structure of the same protein · chain A against A, TM-score 0.45
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 P30870
- Elsewhere: UniProt P30870 · AlphaFold DB P30870
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