Structure of PDB 3uo9 Chain C

Receptor sequence
>3uo9C (length=404) Species: 9606 (Homo sapiens) [Search protein sequence]
LPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLT
LQVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKK
QSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKP
LKYAIAVNDLGTEYVHRYVGKEPSFNKLFLNEDDKPHNPMVNAGAIVVTS
LIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGY
YLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPIT
GERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVP
NVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPR
REGE
3D structure
PDB3uo9 Full-length human glutaminase in complex with an allosteric inhibitor.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S286 K289 Y414 Y466 V484
Catalytic site (residue number reindexed from 1) S146 K149 Y271 Y323 V341
Enzyme Commision number 3.5.1.2: glutaminase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 04A C K320 L321 F322 L323 N324 D327 Y394 K177 L178 F179 L180 N181 D184 Y251 MOAD: ic50=0.08uM
BindingDB: IC50=100nM,Kd=200nM
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
Biological Process
GO:0006541 glutamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3uo9, PDBe:3uo9, PDBj:3uo9
PDBsum3uo9
PubMed22049910
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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