Research workbench
AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (B4RJH7)
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
- B4RJH7
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x57A3AcB7C91DdfC3398a5ED45008eC8bd397c6c0
- UniProt
- B4RJH7
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 521 | — | B4RJH7 |
Compared structures
- 5TW7 · Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae · an experimental structure of the same protein · chain A against C, TM-score 0.93
- 5TW7 · Crystal structure of a GMP synthase (glutamine-hydrolyzing) from Neisseria gonorrhoeae · an experimental structure of the same protein · chain A against C, TM-score 0.93
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 B4RJH7
- Elsewhere: UniProt B4RJH7 · AlphaFold DB B4RJH7
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