Structure of PDB 3uo9 Chain D

Receptor sequence
>3uo9D (length=408) Species: 9606 (Homo sapiens) [Search protein sequence]
LEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQT
TSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESA
KKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCV
KPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGA
IVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRN
FAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGG
FCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGI
LLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAK
KLDPRREE
3D structure
PDB3uo9 Full-length human glutaminase in complex with an allosteric inhibitor.
ChainD
Resolution2.3 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) S148 K151 Y276 Y328 V346
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 F322 L323 N324 E325 Y394 K182 L183 F184 L185 N186 E187 Y256 PDBbind-CN: -logKd/Ki=7.10,IC50=0.08uM
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:3uo9, PDBe:3uo9, PDBj:3uo9
PDBsum3uo9
PubMed22049910
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

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