Structure of PDB 6yjy Chain B

Receptor sequence

>6yjyB (length=329) Species: 9606 (Homo sapiens)

GPAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
TVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGA
RGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELG
LLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTM
DDNEENLDESTIDNLNKILQVFVLEYLHL

3D structure

• PDB: 6yjy Hydrazides Are Potent Transition-State Analogues for Glutaminyl Cyclase Implicated in the Pathogenesis of Alzheimer's Disease.
• Chain: B
• Resolution: 1.67 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 E170 H298
BS02	GLN	B	H140 D159 E201 E202 W207 D248 Q304	H108 D127 E169 E170 W175 D216 Q272
BS03	LEU	B	W207 W329	W175 W297
BS04	TYR	B	V302 Q304	V270 Q272
BS05	PCA	B	E201 E202 W207 Q304	E169 E170 W175 Q272
BS06	TYR	B	V302 Q304	V270 Q272

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:6yjy, PDBe:6yjy, PDBj:6yjy
• PDBsum: 6yjy
• PubMed: 32551535
• UniProt: Q16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)