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S. aureus GS(12) - apo

Analyse S. aureus GS(12) - apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TF7
Type: protein
Length: 4,980 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.13
Source: Staphylococcus aureus
Molecule: Glutamine synthetase
EC: 6.3.1.2
UniProt: E3VXC2
Pockets: 20 · best druggability 0.80

Structure

electron microscopy · resolution 2.13 · 1 distinct chain · 36% helix, 24% 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	415	36% helix, 24% strand	E3VXC2

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	700	0.80	0.85	58	empty
2	682	0.80	0.85	63	empty
3	673	0.80	0.84	60	empty
4	694	0.80	0.84	60	empty
5	655	0.79	0.85	57	empty

Interfaces

24 interfaces between chains.

I–J · 2264 Å² buried · 16 hydrogen bonds · protein-protein
C–K · 2262 Å² buried · 16 hydrogen bonds · protein-protein
G–H · 2254 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 2233 Å² buried · 16 hydrogen bonds · protein-protein
E–F · 2228 Å² buried · 16 hydrogen bonds · protein-protein

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 E3VXC2
Elsewhere: RCSB PDB 7TF7 · PDBe 7TF7 · UniProt E3VXC2

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