Structure of PDB 3vp0 Chain A

Receptor sequence
>3vp0A (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
SMIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTV
DGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLKL
FLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYV
GFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIE
VTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQ
FAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDL
VSLCNFHNYD
3D structure
PDB3vp0 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
Resolution2.4 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 Y193 Y245 V263
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 GLN A Y249 Q285 S286 N335 E381 N388 Y414 Y466 V484 Y31 Q67 S68 N114 E160 N167 Y193 Y245 V263
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:3vp0, PDBe:3vp0, PDBj:3vp0
PDBsum3vp0
PubMed22538822
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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