Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] subunit B (O59072)
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
- O59072
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc68aC5e94B8753FB46682724bd6fC29cf50d2c55
- UniProt
- O59072
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | O59072 |
Compared structures
- 2DPL · Crystal structure of the gmp synthase from pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 2DPL · Crystal Structure of the GMP synthase from Pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 3A4I · Crystal structure of gmp synthetase PH1347 from pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 3A4I · Crystal structure of GMP synthetase PH1347 from Pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 O59072
- Elsewhere: UniProt O59072 · AlphaFold DB O59072
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