Structure of PDB 5uqe Chain D

Receptor sequence
>5uqeD (length=507) Species: 9606 (Homo sapiens) [Search protein sequence]
PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTL
QTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKLVIPDFMSFTSHIDELYE
SAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQS
CVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGD
RNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLAN
GGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAG
GILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDS
RTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVF
KILQEYQ
3D structure
PDB5uqe The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats.
ChainD
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) 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 04A D K320 L321 D327 Y394 K184 L185 D191 Y258 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
View graph for
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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