Structure of PDB 4jkt Chain D

Receptor sequence
>4jktD (length=388) Species: 10090 (Mus musculus) [Search protein sequence]
LEDLLFYTIQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTVML
DKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGK
VADLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVH
RYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFD
YVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTD
MVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLD
KMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRR
3D structure
PDB4jkt Active Glutaminase C Self-assembles into a Supratetrameric Oligomer That Can Be Disrupted by an Allosteric Inhibitor.
ChainD
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) S130 K133 Y258 Y310 V328
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 D R322 K325 L326 F327 L328 N329 E330 Y399 R161 K164 L165 F166 L167 N168 E169 Y238 PDBbind-CN: -logKd/Ki=7.09,IC50=80.4nM
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
Biological Process
GO:0006541 glutamine metabolic process

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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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