2ojw Summary


Crystal structure of human glutamine synthetase in complex with ADP and phosphate

The structure was published by Krajewski, W.W., Collins, R., Holmberg-Schiavone, L., Jones, T.A., Karlberg, T., and Mowbray, S.L., in 2008 in a paper entitled "Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.05 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Glutamine synthetase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodecamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Glutamine synthetase P15104 (5-365) (GLNA_HUMAN)search Homo sapienssearch 97% 384 94%
B Glutamine synthetase P15104 (5-365) (GLNA_HUMAN)search Homo sapienssearch 97% 384 94%
C Glutamine synthetase P15104 (5-365) (GLNA_HUMAN)search Homo sapienssearch 97% 384 94%
D Glutamine synthetase P15104 (5-365) (GLNA_HUMAN)search Homo sapienssearch 97% 384 94%
E Glutamine synthetase P15104 (5-365) (GLNA_HUMAN)search Homo sapienssearch 97% 384 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15104 (5 - 365) Glutamine synthetase Homo sapiens

Chain Sequence family (Pfam)
A, B, C, D, E (P15104) PF00120: Glutamine synthetase, catalytic domainsearch, PF03951: Glutamine synthetase, beta-Grasp domainsearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A, B, C, D, E (P15104) glutamine biosynthetic processsearch cell proliferationsearch cellular nitrogen compound metabolic processsearch synaptic transmissionsearch nitrogen compound metabolic processsearch positive regulation of epithelial cell proliferationsearch cellular response to starvationsearch response to glucosesearch cellular amino acid biosynthetic processsearch glutamate metabolic processsearch glutamate catabolic processsearch neurotransmitter uptakesearch protein homooligomerizationsearch positive regulation of synaptic transmission, glutamatergicsearch positive regulation of insulin secretionsearch small molecule metabolic processsearch extracellular vesicular exosomesearch neuron projectionsearch perikaryonsearch cytoplasmsearch cell projectionsearch protein complexsearch glial cell projectionsearch cell bodysearch intracellular membrane-bounded organellesearch rough endoplasmic reticulumsearch mitochondrionsearch nucleussearch axon terminussearch cytosolsearch identical protein bindingsearch glutamate-ammonia ligase activitysearch ligase activitysearch glutamate decarboxylase activitysearch catalytic activitysearch glutamate bindingsearch ATP bindingsearch manganese ion bindingsearch dynein light chain bindingsearch magnesium ion bindingsearch lyase activitysearch nucleotide bindingsearch

Chain InterPro annotation
A, B, C, D, E Glutamine synthetase, catalytic domainsearch Glutamine synthetase, beta-Graspsearch Glutamine synthetase/guanido kinase, catalytic domainsearch Glutamine synthetase, N-terminal conserved sitesearch Glutamine synthetase, glycine-rich sitesearch