Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] subunit a (Q58970)
Analyse AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q58970
- Type
- protein
- Length
- 188 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- UniProt
- Q58970
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 188 | — | Q58970 |
Compared structures
- 7D95 · Crystal structure of acivicin-bound GATase subunit of Methanocaldococcus jannaschii GMP… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 7D40 · Crystal structure of GATase subunit of Methanocaldococcus jannaschii GMP synthetase · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 8GR3 · Crystal structure of K151L/Y158F mutant of GATase subunit of Methanocaldococcus… · an experimental structure of the same protein · chain A against D, TM-score 0.98
- 8GR1 · Crystal structure of D110V/K151L mutant of GATase subunit of Methanocaldococcus… · an experimental structure of the same protein · chain A against D, TM-score 0.98
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 Q58970
- Elsewhere: UniProt Q58970 · AlphaFold DB Q58970
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