MolNFT v1 · #38070 · protein
Refined atomic model of glutamine synthetase at 3.5 ångströms resolution
2GLS: “Refined atomic model of glutamine synthetase at 3.5 ångströms resolution”. X-ray diffraction, 1 ligand (MN), 20 pockets (best druggability 0.81). MolNFT v1 #38070 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GLS
- Type
- protein
- Length
- 5,616 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2
- UniProt
- P0A1P6
- Ligands
- MN
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% 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 | 468 | 33% helix, 18% strand | P0A1P6 |
Ligands and binding sites
- 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 | 979 | 0.81 | 0.82 | 86 | MN |
| 2 | 979 | 0.80 | 0.82 | 87 | MN |
| 3 | 1127 | 0.80 | 0.81 | 93 | MN |
| 4 | 1074 | 0.79 | 0.81 | 85 | MN |
| 5 | 1127 | 0.79 | 0.81 | 86 | MN |
Interfaces
24 interfaces between chains.
- F–L · 2736 Ų buried · 24 hydrogen bonds · protein-protein
- E–K · 2735 Ų buried · 24 hydrogen bonds · protein-protein
- B–H · 2734 Ų buried · 24 hydrogen bonds · protein-protein
- C–I · 2734 Ų buried · 24 hydrogen bonds · protein-protein
- D–J · 2733 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2GLS · Refined atomic model of glutamine synthetase at 3.5 ångströms resolution · the same entry in another collection · chain L against L, 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 P0A1P6
- Elsewhere: RCSB PDB 2GLS · PDBe 2GLS · UniProt P0A1P6
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