Research workbench
Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme
Analyse Structural studies on the synchronization of catalytic centers in glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LM1
- Type
- protein
- Length
- 1,475 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-dependent glutamate synthase
- EC
- 1.4.7.1
- UniProt
- P55038
- Ligands
- FMN, F3S
- Pockets
- 19 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-dependent glutamate synthase (EC 1.4.7.1) | protein | 1475 | 36% helix, 17% strand | P55038 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- F3S · FE3-S4 cluster · ligand · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.84 | 0.96 | 52 | empty |
| 2 | 225 | 0.82 | 0.95 | 50 | ACT, FMN |
| 3 | 568 | 0.70 | 0.80 | 55 | empty |
| 4 | 57 | 0.65 | 0.95 | 19 | empty |
| 5 | 110 | 0.65 | 0.89 | 22 | empty |
Compared structures
- 1LM1 · Structural studies on the synchronization of catalytic centers in glutamate synthase… · the same entry in another collection · chain A against A, TM-score 1.00
- P55038 · AlphaFold monomer V2.0 prediction for ferredoxin-dependent glutamate synthase 2 (P55038) · 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 P55038
- Elsewhere: RCSB PDB 1LM1 · PDBe 1LM1 · UniProt P55038
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