Structure of PDB 8xgt Chain F

Receptor sequence
>8xgtF (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEEN
LDESTIDNLNKILQVFVLEYLHL
3D structure
PDB8xgt X-ray Structure-Guided Discovery of a Potent Benzimidazole Glutaminyl Cyclase Inhibitor That Shows Activity in a Parkinson's Disease Mouse Model.
ChainF
Resolution2.813 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.5: glutaminyl-peptide cyclotransferase.
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 ZN F D159 E202 H330 D127 E164 H292
BS02 A1D48 F D159 E202 W207 D248 Q304 W329 H330 D127 E164 W169 D210 Q266 W291 H292
BS03 A1D48 F P262 N263 P224 N225
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016603 glutaminyl-peptide cyclotransferase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0017186 peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
GO:0036211 protein modification process
Cellular Component
GO:0005576 extracellular region
GO:0035580 specific granule lumen
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8xgt, PDBe:8xgt, PDBj:8xgt
PDBsum8xgt
PubMed38817193
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

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