Structure of PDB 4jkt Chain A

Receptor sequence
>4jktA (length=395) Species: 10090 (Mus musculus) [Search protein sequence]
LEDLLFYTIKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLVMLDKDL
FKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADY
IPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVND
LGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGV
NNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKK
CFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLS
PEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMM
CWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRR
3D structure
PDB4jkt Active Glutaminase C Self-assembles into a Supratetrameric Oligomer That Can Be Disrupted by an Allosteric Inhibitor.
ChainA
Resolution2.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S291 K294 Y419 Y471 V489
Catalytic site (residue number reindexed from 1) S137 K140 Y265 Y317 V335
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 A K325 L326 F327 L328 N329 E330 Y399 K171 L172 F173 L174 N175 E176 Y245 PDBbind-CN: -logKd/Ki=7.09,IC50=80.4nM
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:4jkt, PDBe:4jkt, PDBj:4jkt
PDBsum4jkt
PubMed23935106
UniProtD3Z7P3|GLSK_MOUSE Glutaminase kidney isoform, mitochondrial (Gene Name=Gls)

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