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Crystal structure of the N-terminal degron-truncated human glutamine synthetase
Analyse Crystal structure of the N-terminal degron-truncated human glutamine synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EVT
- Type
- protein
- Length
- 3,392 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.95
- Source
- Homo sapiens
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2, 2.3.1.225
- UniProt
- P15104
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · resolution 2.95 · 10 distinct chains · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 341 | 27% helix, 26% strand | P15104 |
| B | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 344 | 28% helix, 26% strand | P15104 |
| C | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 341 | 28% helix, 26% strand | P15104 |
| D | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 335 | 26% helix, 27% strand | P15104 |
| E | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 316 | 29% helix, 25% strand | P15104 |
| F | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 340 | 29% helix, 26% strand | P15104 |
| G | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 342 | 29% helix, 26% strand | P15104 |
| H | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 348 | 27% helix, 26% strand | P15104 |
| I | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 342 | 26% helix, 26% strand | P15104 |
| J | Glutamine synthetase (EC 6.3.1.2, 2.3.1.225) | protein | 343 | 27% helix, 26% strand | P15104 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 979 | 0.77 | 0.80 | 84 | empty |
| 2 | 902 | 0.76 | 0.79 | 90 | empty |
| 3 | 987 | 0.75 | 0.78 | 113 | empty |
| 4 | 795 | 0.75 | 0.80 | 75 | empty |
| 5 | 890 | 0.75 | 0.79 | 83 | empty |
Interfaces
20 interfaces between chains.
- G–H · 1341 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1301 Ų buried · 23 hydrogen bonds · protein-protein
- F–J · 1265 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1237 Ų buried · 25 hydrogen bonds · protein-protein
- H–I · 1233 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 7EVT · Crystal structure of the N-terminal degron-truncated human glutamine synthetase · the same entry in another collection · chain J against J, TM-score 1.00
- P15104 · AlphaFold monomer V2.0 prediction for glutamine synthetase (P15104) · a predicted model of the same protein · chain C 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 P15104
- Elsewhere: RCSB PDB 7EVT · PDBe 7EVT · UniProt P15104
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