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Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to 3.5 Angstrom
Analyse Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TEN
- Type
- protein
- Length
- 5,304 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.5
- Source
- Listeria monocytogenes
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2
- UniProt
- A0A5D5GA79
- Ligands
- ADP, P3S
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · resolution 3.5 · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, B, D, H, J, M, O, Q, S, U, W | Glutamine synthetase (EC 6.3.1.2) | protein | 442 | 33% helix, 21% strand | A0A5D5GA79 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 12 copies · chains A, E, Q, B, D, H, J, U, M, O, S, W
- P3S · L-methionine-S-sulfoximine phosphate · ligand · 12 copies · chains A, E, Q, B, D, H, J, U, M, O, S, W
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 | 356 | 0.81 | 0.91 | 54 | ADP, P3S |
| 2 | 319 | 0.81 | 0.91 | 46 | ADP |
| 3 | 359 | 0.80 | 0.90 | 58 | ADP, P3S |
| 4 | 343 | 0.80 | 0.90 | 55 | ADP, P3S |
| 5 | 321 | 0.80 | 0.91 | 52 | ADP, P3S |
Interfaces
24 interfaces between chains.
- H–O · 2111 Ų buried · 18 hydrogen bonds · protein-protein
- E–B · 2022 Ų buried · 18 hydrogen bonds · protein-protein
- Q–W · 2017 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 2016 Ų buried · 21 hydrogen bonds · protein-protein
- J–M · 1993 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 covalent (covalent ligand).
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 A0A5D5GA79
- Elsewhere: RCSB PDB 7TEN · PDBe 7TEN · UniProt A0A5D5GA79
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