Structure of PDB 3vp4 Chain A Binding Site BS01

Receptor Information

>3vp4 Chain A (length=312) Species: 9606 (Homo sapiens)

QSMIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCT
VDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLN
KLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNE
YVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCS
IEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFS
GQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCH
DLVSLCNFHNYD

Ligand information

• Ligand ID: BP9
• InChI: InChI=1S/C8H12N6S2/c9-7-13-11-5(15-7)3-1-2-4-6-12-14-8(10)16-6/h1-4H2,(H2,9,13)(H2,10,14)
• InChIKey: FXLSMCSUYSZCFA-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.370: Nc1sc(CCCCc2sc(N)nn2)nn1
  OpenEye OEToolkits 1.7.6: C(CCc1nnc(s1)N)Cc2nnc(s2)N
  ACDLabs 12.01: n1nc(sc1CCCCc2nnc(s2)N)N
• Formula: C8 H12 N6 S2
• Name: 5,5'-butane-1,4-diylbis(1,3,4-thiadiazol-2-amine)
• ZINC: ZINC000095837056
• PDB chain: 3vp4 Chain A Residue 601

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3vp4 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.
• Resolution: 2.45 Å
• Binding residue (original residue number in PDB): L323 Y394
• Binding residue (residue number reindexed from 1): L104 Y175
• Annotation score: 1
• Binding affinity: PDBbind-CN: -logKd/Ki=4.73,IC50=18.6uM

Enzymatic activity

• Catalytic site (original residue number in PDB): S286 K289 Y414 Y466 V484
• Catalytic site (residue number reindexed from 1): S69 K72 Y195 Y247 V265
• Enzyme Commision number: 3.5.1.2: glutaminase.

Gene Ontology

Molecular Function

• GO:0004359 glutaminase activity

Biological Process

• GO:0006541 glutamine metabolic process

External links

• PDB: RCSB:3vp4, PDBe:3vp4, PDBj:3vp4
• PDBsum: 3vp4
• PubMed: 22538822
• UniProt: O94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)