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Ligands
Code Name Style Show Link
04A N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide)
GLU Glutamic acid
SO4 Sulfate ion
Non-standard Residues
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Code : 3VP1   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure of human glutaminase in complex with L-glutamate and BPTES
Release Data : 2012-06-13
Compound :
mol_id molecule chains synonym
1 Glutaminase kidney isoform, mitochondrial A GLS, K-glutaminase, L-glutamine amidohydrolase
ec: 3.5.1.2
fragment: UNP Residues 221-533
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: GLS, GLS1, KIAA0838
Authors : Thangavelu, K., Sivaraman, J.
Keywords : HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Structural basis for the allosteric inhibitory mechanism of human kidney-type glutaminase (KGA) and its regulation by Raf-Mek-Erk signaling in cancer cell metabolism.

Thangavelu, K.,Pan, C.Q.,Karlberg, T.  et al.
(2012)  Proc.Natl.Acad.Sci.USA  109 : 7705 - 7710

PubMed: 22538822
DOI: 10.1073/pnas.1116573109

Chain : A
UniProt : O94925 (GLSK_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + L-glutamine = L-glutamate + NH4(+) 3.5.1.2 PubMed:22049910, PubMed:22538822, PubMed:24451979, PubMed:26988803, PubMed:28526749, PubMed:29317493
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