Structure of PDB 3vp2 Chain A

Receptor sequence
>3vp2A (length=311) Species: 9606 (Homo sapiens) [Search protein sequence]
SMIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTV
DGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLNK
LFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEY
VGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSI
EVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSG
QFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHD
LVSLCNFHNYD
3D structure
PDB3vp2 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.
ChainA
Resolution2.7 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) S68 K71 Y194 Y246 V264
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 BP0 A L323 Y394 L103 Y174 PDBbind-CN: -logKd/Ki=5.10,IC50=8.02uM
BindingDB: IC50=100000nM
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:3vp2, PDBe:3vp2, PDBj:3vp2
PDBsum3vp2
PubMed22538822
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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