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 Not available
Homo sapienssearch 97% 384 94%
B Glutamine synthetase Not available
Homo sapienssearch 97% 384 94%
C Glutamine synthetase Not available
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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B, C, D, E (P15104) catalytic activitysearch ATP bindingsearch dynein light chain bindingsearch magnesium ion bindingsearch lyase activitysearch nucleotide bindingsearch glutamate decarboxylase activitysearch ligase activitysearch glutamate bindingsearch manganese ion bindingsearch identical protein bindingsearch glutamate-ammonia ligase activitysearch synaptic transmissionsearch positive regulation of synaptic transmission, glutamatergicsearch positive regulation of insulin secretionsearch glutamate catabolic processsearch protein homooligomerizationsearch cellular amino acid biosynthetic processsearch positive regulation of epithelial cell proliferationsearch small molecule metabolic processsearch neurotransmitter uptakesearch glutamine biosynthetic processsearch cellular response to starvationsearch response to glucosesearch cellular nitrogen compound metabolic processsearch cell proliferationsearch nitrogen compound metabolic processsearch glutamate metabolic processsearch mitochondrionsearch cytoplasmsearch perikaryonsearch intracellular membrane-bounded organellesearch protein complexsearch nucleussearch cell projectionsearch neuron projectionsearch rough endoplasmic reticulumsearch cell bodysearch axon terminussearch extracellular vesicular exosomesearch cytosolsearch glial cell projectionsearch

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