Structure of PDB 3si2 Chain A

Receptor sequence
>3si2A (length=322) Species: 10090 (Mus musculus) [Search protein sequence]
AWTQEKNHHQPAHLNSSSLQQVAEGTSISEMWQNDLRPLLIERYPGSPGS
YSARQHIMQRIQRLQAEWVVEVDTFLSRTPYGYRSFSNIISTLNPEAKRH
LVLACHYDSKYFPRWDSRVFVGATDSAVPCAMMLELARALDKKLHSLKDP
DLSLQLIFFDGEEAFHHWSPQDSLYGSRHLAQKMASSPHPPGSRGTNQLD
GMDLLVLLDLIGAANPTFPNFFPKTTRWFNRLQAIEKELYELGLLKDHSL
ERKYFQNFGYGNIIQDDHIPFLRKGVPVLHLIASPFPEVWHTMDDNEENL
HASTIDNLNKIIQVFVLEYLHL
3D structure
PDB3si2 Structures of Glycosylated Mammalian Glutaminyl Cyclases Reveal Conformational Variability near the Active Center.
ChainA
Resolution1.8 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 D160 E203 H331 D125 E163 H291
BS02 PBD A D160 E202 E203 W208 D249 N302 I304 Q305 F326 H331 D125 E162 E163 W168 D209 N262 I264 Q265 F286 H291 MOAD: ic50=3nM
Gene Ontology
Molecular Function
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
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:3si2, PDBe:3si2, PDBj:3si2
PDBsum3si2
PubMed21671571
UniProtQ9CYK2|QPCT_MOUSE Glutaminyl-peptide cyclotransferase (Gene Name=Qpct)

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