Structure of PDB 3vp1 Chain A

Receptor sequence
>3vp1A (length=313) Species: 9606 (Homo sapiens) [Search protein sequence]
SMIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTV
DGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRF
NKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGN
EYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLC
SIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDF
SGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFC
HDLVSLCNFHNYD
3D structure
PDB3vp1 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
Resolution2.3 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) S68 K71 Y196 Y248 V266
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 R317 F318 L321 L323 N324 E325 Y394 R99 F100 L103 L105 N106 E107 Y176 PDBbind-CN: -logKd/Ki=5.48,IC50=3.3uM
BindingDB: IC50=100nM,Kd=200nM
BS02 GLU A Y249 Q285 S286 N335 E381 Y414 Y466 V484 Y31 Q67 S68 N117 E163 Y196 Y248 V266
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
Biological Process
GO:0006541 glutamine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3vp1, PDBe:3vp1, PDBj:3vp1
PDBsum3vp1
PubMed22538822
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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