Research workbench
Saccharomyces cerevisiae glutamate cysteine ligase in complex with MG2+, L-glutamate and ADP
Analyse Saccharomyces cerevisiae glutamate cysteine ligase in complex with MG2+… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IG8
- Type
- protein
- Length
- 672 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate-cysteine ligase
- EC
- 6.3.2.2
- UniProt
- P32477
- Ligands
- GLU, ADP, MG
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate-cysteine ligase (EC 6.3.2.2) | protein | 672 | 41% helix, 13% strand | P32477 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 763 | 0.73 | 0.79 | 66 | GLU, ADP, MG |
| 2 | 143 | 0.59 | 0.84 | 26 | empty |
| 3 | 316 | 0.55 | 0.76 | 32 | empty |
| 4 | 112 | 0.42 | 0.77 | 23 | PGE |
| 5 | 51 | 0.37 | 0.80 | 15 | empty |
Compared structures
- 3IG8 · Saccharomyces cerevisiae glutamate cysteine ligase in complex with Mg2+, L-glutamate and… · the same entry in another collection · chain A against A, TM-score 1.00
- P32477 · AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (P32477) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P32477
- Elsewhere: RCSB PDB 3IG8 · PDBe 3IG8 · UniProt P32477
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