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Glutamine synthetase from drosophila

Analyse Glutamine synthetase from drosophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CPR
Type: protein
Length: 3,658 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P20478
Ligands: ADP

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, F, J	—	protein	367	—	P20478
B	—	protein	366	—	P20478
C, H	—	protein	366	—	P20478
D	—	protein	364	—	P20478
E, G	—	protein	365	—	P20478
I	—	protein	365	—	P20478

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 10 copies · chains A, E, B, C, D, F, J, G, H, I

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7CPR · glutamine synthetase from Drosophila · the same entry in another collection · chain J against J, TM-score 1.00
P20478 · AlphaFold monomer V2.0 prediction for glutamine synthetase 2 cytoplasmic (P20478) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P20478
Elsewhere: RCSB PDB 7CPR · PDBe 7CPR · UniProt P20478

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