Structure of PDB 7d8e Chain A

Receptor sequence
>7d8eA (length=318) Species: 9606 (Homo sapiens) [Search protein sequence]
AWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGS
YAARQHIMQRIQRLQADWVLEIDTFLSQTPEGERSFSNIISTLNPTAKRH
LVLACHYDSKYFSHNRVFVGATDSAVPCAMMLELARALDKKLLSLKDLSL
QLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDL
LVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRY
FQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDEST
IDNLNKILQVFVLEYLHL
3D structure
PDB7d8e Crystal Structure of double mutant Y115E Y117E human Secretory Glutaminyl Cyclase in complex with LSB-09
ChainA
Resolution2.0 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 A D159 E202 H330 D123 E159 H287
BS02 GYO A D159 E201 E202 W207 D248 Q304 W329 H330 D123 E158 E159 W164 D205 Q261 W286 H287
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:7d8e, PDBe:7d8e, PDBj:7d8e
PDBsum7d8e
PubMed
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

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