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Cryoem plasmodium falciparum glutamine synthetase

Analyse Cryoem plasmodium falciparum glutamine synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PEW
Type: protein
Length: 6,252 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamine synthetase
UniProt: A0A2I0BT46
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 28% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, G, H, I, J, K, L, A, B, C, E, F	Glutamine synthetase	protein	521	28% helix, 20% strand	A0A2I0BT46

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	780	0.86	0.89	74	empty
2	824	0.85	0.88	75	empty
3	801	0.85	0.88	73	empty
4	751	0.85	0.89	73	empty
5	798	0.85	0.88	72	empty

Interfaces

24 interfaces between chains.

K–F · 2788 Å² buried · 32 hydrogen bonds · protein-protein
I–A · 2787 Å² buried · 32 hydrogen bonds · protein-protein
G–C · 2786 Å² buried · 32 hydrogen bonds · protein-protein
D–E · 2777 Å² buried · 30 hydrogen bonds · protein-protein
H–B · 2773 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

6PEW · CryoEM Plasmodium falciparum glutamine synthetase · the same entry in another collection · chain D against D, 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 A0A2I0BT46
Elsewhere: RCSB PDB 6PEW · PDBe 6PEW · UniProt A0A2I0BT46

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