Structure of PDB 6ujg Chain E

Receptor sequence
>6ujgE (length=410) Species: 9606 (Homo sapiens) [Search protein sequence]
PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTL
QTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYE
SAKKQSGGKVADYIPQLAKFSPDLWGVSVCTADGQRHSTGDTKVPFCLQS
CVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGD
RNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLAN
GGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAG
GILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
3D structure
PDB6ujg Characterization of the interactions of potent allosteric inhibitors with glutaminase C, a key enzyme in cancer cell glutamine metabolism.
ChainE
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S286 K289 Y414 Y466 V484
Catalytic site (residue number reindexed from 1) S150 K153 Y278 Y330 V348
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 Q9A E K320 L321 L323 Y394 K184 L185 L187 Y258 BindingDB: IC50=7700nM
Gene Ontology
Molecular Function
GO:0004359 glutaminase activity
Biological Process
GO:0006541 glutamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6ujg, PDBe:6ujg, PDBj:6ujg
PDBsum6ujg
PubMed
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

[Back to BioLiP]