Structure of PDB 5uqe Chain F

Receptor sequence
>5uqeF (length=407) Species: 9606 (Homo sapiens) [Search protein sequence]
SLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ
TTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKLVIPDFMSFTSHIDELYES
AKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSC
VKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAG
AIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR
NFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANG
GFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGG
ILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFA
KKLDPRR
3D structure
PDB5uqe The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats.
ChainF
Resolution3.6 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
Catalytic site (residue number reindexed from 1) S149
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 F F318 K320 L321 F322 E325 Y394 F181 K183 L184 F185 E188 Y257 BindingDB: IC50=100nM,Kd=200nM
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:5uqe, PDBe:5uqe, PDBj:5uqe
PDBsum5uqe
PubMed28526749
UniProtO94925|GLSK_HUMAN Glutaminase kidney isoform, mitochondrial (Gene Name=GLS)

[Back to BioLiP]