Structure of PDB 7cm0 Chain A

Receptor sequence
>7cm0A (length=321) Species: 9606 (Homo sapiens) [Search protein sequence]
AWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGS
YAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRH
LVLACHYDSKYFSNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVPD
LSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG
MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLE
GRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLD
ESTIDNLNKILQVFVLEYLHL
3D structure
PDB7cm0 Discovery of highly potent human glutaminyl cyclase (QC) inhibitors as anti-Alzheimer's agents by the combination of pharmacophore-based and structure-based design.
ChainA
Resolution2.2 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 G5R A D159 E201 D248 Q304 D305 F325 P326 E327 W329 H330 D123 E161 D208 Q264 D265 F285 P286 E287 W289 H290
BS02 ZN A D159 E202 H330 D123 E162 H290
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:7cm0, PDBe:7cm0, PDBj:7cm0
PDBsum7cm0
PubMed34536669
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

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