Structure of PDB 2afx Chain A Binding Site BS02

Receptor Information
>2afx Chain A (length=323) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEEN
LDESTIDNLNKILQVFVLEYLHL
Ligand information
Ligand ID1BN
InChIInChI=1S/C10H10N2/c1-2-4-10(5-3-1)8-12-7-6-11-9-12/h1-7,9H,8H2
InChIKeyKKKDZZRICRFGSD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C(n1ccnc1)c2ccccc2
OpenEye OEToolkits 1.5.0c1ccc(cc1)Cn2ccnc2
ACDLabs 10.04n1ccn(c1)Cc2ccccc2
FormulaC10 H10 N2
Name1-BENZYL-1H-IMIDAZOLE;
1-BENZYLIMIDAZOLE
ChEMBLCHEMBL14192
DrugBankDB04581
ZINCZINC000000169811
PDB chain2afx Chain A Residue 1501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2afx Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
Resolution1.64 Å
Binding residue
(original residue number in PDB)		D159 E201 E202 D248 Q304 F325 W329 H330
Binding residue
(residue number reindexed from 1)		D127 E163 E164 D210 Q266 F287 W291 H292
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.15,Ki=7.1uM
BindingDB: Ki=262nM
Enzymatic activity
Enzyme Commision number 2.3.2.5: glutaminyl-peptide cyclotransferase.
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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