Structure of PDB 2afz Chain A

Receptor sequence

>2afzA (length=323) Species: 9606 (Homo sapiens)

ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEEN
LDESTIDNLNKILQVFVLEYLHL

3D structure

• PDB: 2afz Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
• Chain: A
• Resolution: 1.68 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	A	D159 E202 H330	D127 E164 H292
BS02	NVI	A	D159 E201 E202 D248 Q304 D305 I321 H330	D127 E163 E164 D210 Q266 D267 I283 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:2afz, PDBe:2afz, PDBj:2afz
• PDBsum: 2afz
• PubMed: 16135565
• UniProt: Q16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)