Structure of PDB 6gbx Chain B

Receptor sequence
>6gbxB (length=328) Species: 9606 (Homo sapiens) [Search protein sequence]
SAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPG
SYAARQHIMQRIQRLQADWVLEIDTFLSQTPEGERSFSNIISTLNPTAKR
HLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKT
VSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGAR
GTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGL
LKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMD
DNEENLDESTIDNLNKILQVFVLEYLHL
3D structure
PDB6gbx 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.
ChainB
Resolution1.72 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 B D159 E202 H330 D126 E169 H297
BS02 S77 B K144 D159 E201 W207 D248 Q304 D305 W329 H330 K111 D126 E168 W174 D215 Q271 D272 W296 H297 MOAD: Ki=0.02uM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6gbx, PDBe:6gbx, PDBj:6gbx
PDBsum6gbx
PubMed30132075
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

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