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Glutamine synthetase assignment by UMBC undergraduate studentsGlutamine synthetase assignment by UMBC undergraduate students

spinqualitylabelsall models PDB ID 2gls Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2gls, resolution 3.50Å ()
Ligands:
Activity:	Glutamate--ammonia ligase, with EC number 6.3.1.2
Structural annotation: Resources: CATH : 2Glsa02, 2Glsa01, 2Glsb02, 2Glsb01, 2Glsc01, 2Glsc02, 2Glsd02, 2Glsd01, 2Glse02, 2Glse01, 2Glsf02, 2Glsf01, 2Glsg01, 2Glsg02, 2Glsh02, 2Glsh01, 2Glsi02, 2Glsi01, 2Glsj01, 2Glsj02, 2Glsk01, 2Glsk02, 2Glsl02, 2Glsl01 InterPro : Ipr014746, Ipr008146, Ipr001637, Ipr008147, Ipr004809 Pfam : PF00120, PF03951 SCOP : d2glsa2, d2glsa1, d2glsb2, d2glsb1, d2glsc1, d2glsc2, d2glsd2, d2glsd1, d2glse2, d2glse1, d2glsf1, d2glsf2, d2glsg2, d2glsg1, d2glsh2, d2glsh1, d2glsi2, d2glsi1, d2glsj2, d2glsj1, d2glsk1, d2glsk2, d2glsl2, d2glsl1 UniProt : P0A1P6
Functional annotation: Cellular component: cytoplasm Biological process: nitrogen compound metabolic process glutamine biosynthetic process nitrogen fixation Molecular function: ligase activity nucleotide binding glutamate-ammonia ligase activity catalytic activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

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Glutamine synthetase of Salmonella

Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [1] and has two domains in refined atomic model of glutamine synthetase from Salmonella typhimurium. Hydrophobic interaction is a major driving force determining the most tertiary structure of the proteins. [2] Hydrogen bonding is crucial in stabilizing the tertiary structure as well. [3] Also, disulfide bonds between cysteine residues stabilize the tertiary structure. [4] However, for glutamine synthetase for Salmonella, the most important interaction will be the helix-helix interactions.

Glutamine synthetase from Salmonella has twenty three helix-helix interactions and is four different types of interactions. [5] on the protein residues and regions of the protein residues are represented by deep blue color.

is within uncharged polar <insert wiki showing the uncharged polar groups>. Usually, uncharged polar groups are classified as hydrophilic <insert wiki showing the hydrophilic> that is found on the outside of proteins. Also, amino acids with the character of acidic or basic side chains are polar, showing on the outside of molecules <insert wiki showing the polar>. For glutamine, its side chain is uncharged and formed by replacing the hydroxyl of glutamic acid with an amine functional group. [6] In the other hand, glutamine has no side chain on non-polar group, however the side chain on non-polar groups of the proteins usually tends to be hydrophobic <insert wiki showing the hydrophobic of cysteine> and to cluster together on the inside.[7]