MolNFT v1 · #13587 · protein
Interactions of nucleotides with fully unadenylylated glutamine synthetase from salmonella typhimurium
1LGR: “Interactions of nucleotides with fully unadenylylated glutamine synthetase from salmonella typhimurium”. X-ray diffraction, 2 ligands (AMP, MN), 20 pockets (best druggability 0.78). MolNFT v1 #13587 on GenesisL1: 3D structure…
- PDB
- 1LGR
- 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
- AMP, MN
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% 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 | 38% helix, 23% strand | P06201 |
Ligands and binding sites
- AMP · Adenosine monophosphate · 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 | 28 | empty |
| 2 | 372 | 0.78 | 0.88 | 35 | empty |
| 3 | 970 | 0.77 | 0.80 | 76 | AMP |
| 4 | 369 | 0.77 | 0.88 | 38 | empty |
| 5 | 994 | 0.77 | 0.80 | 80 | MN, AMP |
Interfaces
24 interfaces between chains.
- A–G · 2823 Ų buried · 32 hydrogen bonds · protein-protein
- F–H · 2822 Ų buried · 32 hydrogen bonds · protein-protein
- E–I · 2821 Ų buried · 32 hydrogen bonds · protein-protein
- B–L · 2814 Ų buried · 32 hydrogen bonds · protein-protein
- C–K · 2812 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 1LGR · Interactions of nucleotides with fully unadenylylated glutamine synthetase from… · the same entry in another collection · 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 P06201
- Elsewhere: RCSB PDB 1LGR · PDBe 1LGR · UniProt P06201
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