Structure of PDB 6gbx Chain A

Receptor sequence

>6gbxA (length=328) Species: 9606 (Homo sapiens)

SAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPG
SYAARQHIMQRIQRLQADWVLEIDTFLSQTPEGERSFSNIISTLNPTAKR
HLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKT
VSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGAR
GTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGL
LKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMD
DNEENLDESTIDNLNKILQVFVLEYLHL

3D structure

• PDB: 6gbx The structure of the human glutaminyl cyclase-SEN177 complex indicates routes for developing new potent inhibitors as possible agents for the treatment of neurological disorders.
• Chain: A
• Resolution: 1.72 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	D126 E169 H297
BS02	S77	A	K144 D159 E201 W207 D248 Q304 D305 W329 H330	K111 D126 E168 W174 D215 Q271 D272 W296 H297	MOAD: Ki=0.02uM PDBbind-CN: -logKd/Ki=7.70,Ki=0.020uM BindingDB: IC50=17nM

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:6gbx, PDBe:6gbx, PDBj:6gbx
• PDBsum: 6gbx
• PubMed: 30132075
• UniProt: Q16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)