Research workbench
AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (B4TT00)
Analyse AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (B4TT00) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4TT00
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x61A3874B0aD51eD2238D4A705d4a267bA385D206
- Molecule
- Glutamate--cysteine ligase
- UniProt
- B4TT00
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--cysteine ligase | protein | 518 | 50% helix, 13% strand | B4TT00 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.76 | 0.88 | 31 | empty |
| 2 | 926 | 0.74 | 0.77 | 89 | empty |
| 3 | 140 | 0.45 | 0.76 | 21 | empty |
| 4 | 67 | 0.40 | 0.79 | 15 | empty |
| 5 | 76 | 0.38 | 0.77 | 17 | 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 B4TT00
- Elsewhere: UniProt B4TT00 · AlphaFold DB B4TT00
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