Research workbench
Feedback inhibition of fully unadenylylated glutamine synthetase from salmonella typhimurium by glycine, alanine, and serine
Analyse Feedback inhibition of fully unadenylylated glutamine synthetase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LGS
- Type
- protein
- Length
- 5,340 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2
- UniProt
- P06201
- Ligands
- GLU, MN
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Glutamine synthetase (EC 6.3.1.2) | protein | 445 | 37% helix, 23% strand | P06201 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- MN · Manganese (II) ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.78 | 0.89 | 27 | empty |
| 2 | 375 | 0.78 | 0.88 | 35 | empty |
| 3 | 335 | 0.78 | 0.88 | 26 | empty |
| 4 | 993 | 0.78 | 0.80 | 76 | MN, GLU |
| 5 | 973 | 0.77 | 0.80 | 77 | MN, GLU |
Interfaces
24 interfaces between chains.
- A–G · 2829 Ų buried · 32 hydrogen bonds · protein-protein
- E–I · 2828 Ų buried · 32 hydrogen bonds · protein-protein
- B–L · 2828 Ų buried · 32 hydrogen bonds · protein-protein
- F–H · 2822 Ų buried · 32 hydrogen bonds · protein-protein
- C–K · 2815 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 2LGS · Feedback inhibition of fully unadenylylated glutamine synthetase from salmonella… · the same entry in another collection · chain F against F, 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 P06201
- Elsewhere: RCSB PDB 2LGS · PDBe 2LGS · UniProt P06201
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