Research workbench
Crystal structure of plant glutamate cysteine ligase in complex with MG2+ and L-glutamate
Analyse Crystal structure of plant glutamate cysteine ligase in complex with MG2+ and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GWD
- Type
- protein
- Length
- 436 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
- O23736
- Ligands
- GLU, MG
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate cysteine ligase (EC 6.3.2.2) | protein | 436 | 50% helix, 19% strand | O23736 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.71 | 0.80 | 60 | MG, ACT, GLU |
| 2 | 85 | 0.32 | 0.73 | 21 | ACT |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2GWD · Crystal structure of plant glutamate cysteine ligase in complex with Mg2+ and L-glutamate · the same entry in another collection · chain A against A, TM-score 1.00
- O23736 · AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase, chloroplastic (O23736) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 O23736
- Elsewhere: RCSB PDB 2GWD · PDBe 2GWD · UniProt O23736
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