Structure of PDB 2afx Chain A

Receptor sequence
>2afxA (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEEN
LDESTIDNLNKILQVFVLEYLHL
3D structure
PDB2afx Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
ChainA
Resolution1.64 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 D127 E164 H292
BS02 1BN A D159 E201 E202 D248 Q304 F325 W329 H330 D127 E163 E164 D210 Q266 F287 W291 H292 PDBbind-CN: -logKd/Ki=5.15,Ki=7.1uM
BindingDB: Ki=262nM
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:2afx, PDBe:2afx, PDBj:2afx
PDBsum2afx
PubMed16135565
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

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