Structure of PDB 8xgb Chain B

Receptor sequence

>8xgbB (length=323) Species: 9606 (Homo sapiens)

ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEEN
LDESTIDNLNKILQVFVLEYLHL

3D structure

• PDB: 8xgb X-ray Structure-Guided Discovery of a Potent Benzimidazole Glutaminyl Cyclase Inhibitor That Shows Activity in a Parkinson's Disease Mouse Model.
• Chain: B
• Resolution: 3.24 Å

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	B	D159 E202 H330	D127 E164 H292
BS02	A1D49	B	E201 E202 W207 F325 W329 H330	E163 E164 W169 F287 W291 H292

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

External links

• PDB: RCSB:8xgb, PDBe:8xgb, PDBj:8xgb
• PDBsum: 8xgb
• PubMed: 38817193
• UniProt: Q16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)