Sandbox108

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

OUTLINEOUTLINE

Tertiary Structure

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 <insert wiki showing the H.B> is crucial in stabilizing the tertiary structure as well. [3] Also, disulfide bonds <insert wiki showing the disulfide bonds of cysteine> between cysteine residues stabilize the tertiary structure. [4]

Glutamine synthetase from Salmonella has twenty three helix-helix interactions and is four different types of interactions. [5] on the protein residues and polar <polar wiki> (put color) region is represented by gray and light purple, and this characteristic strenthens the folding of proteins. And, it has charged region in the inside of molecules as well.

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]