Structure of PDB 5uqe Chain C

Receptor sequence
>5uqeC (length=484) Species: 9606 (Homo sapiens) [Search protein sequence]
SLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ
TTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKLVIPDFMSFTSHIDELYES
AKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSC
VKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAG
AIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR
NFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANG
GFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGG
ILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFA
KKLDPRRVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAE
GHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHF
3D structure
PDB5uqe The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats.
ChainC
Resolution3.6 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) S149 K152 Y277 Y329 V347
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 C K320 L321 F322 Y394 K183 L184 F185 Y257 BindingDB: IC50=100nM,Kd=200nM
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:5uqe, PDBe:5uqe, PDBj:5uqe
PDBsum5uqe
PubMed28526749
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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