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AlphaFold monomer V2.0 prediction for putative glutamate synthase [NADPH] (Q9C102)
Analyse AlphaFold monomer V2.0 prediction for putative glutamate synthase [NADPH]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C102
- Type
- protein
- Length
- 2,111 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Putative glutamate synthase [NADPH]
- UniProt
- Q9C102
- Pockets
- 20 · best druggability 0.81
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative glutamate synthase [NADPH] | protein | 2111 | 38% helix, 18% strand | Q9C102 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.81 | 0.87 | 83 | empty |
| 2 | 1115 | 0.81 | 0.82 | 110 | empty |
| 3 | 541 | 0.79 | 0.86 | 61 | empty |
| 4 | 746 | 0.75 | 0.80 | 68 | empty |
| 5 | 83 | 0.74 | 0.97 | 26 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9C102
- Elsewhere: UniProt Q9C102 · AlphaFold DB Q9C102
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