Structure of PDB 3si2 Chain A Binding Site BS01

Receptor Information

>3si2 Chain A (length=322) Species: 10090 (Mus musculus)

AWTQEKNHHQPAHLNSSSLQQVAEGTSISEMWQNDLRPLLIERYPGSPGS
YSARQHIMQRIQRLQAEWVVEVDTFLSRTPYGYRSFSNIISTLNPEAKRH
LVLACHYDSKYFPRWDSRVFVGATDSAVPCAMMLELARALDKKLHSLKDP
DLSLQLIFFDGEEAFHHWSPQDSLYGSRHLAQKMASSPHPPGSRGTNQLD
GMDLLVLLDLIGAANPTFPNFFPKTTRWFNRLQAIEKELYELGLLKDHSL
ERKYFQNFGYGNIIQDDHIPFLRKGVPVLHLIASPFPEVWHTMDDNEENL
HASTIDNLNKIIQVFVLEYLHL

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 3si2 Chain A Residue 601

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3si2 Structures of Glycosylated Mammalian Glutaminyl Cyclases Reveal Conformational Variability near the Active Center.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D160 E203 H331
• Binding residue (residue number reindexed from 1): D125 E163 H291
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.3.2.5: glutaminyl-peptide cyclotransferase.

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

External links

• PDB: RCSB:3si2, PDBe:3si2, PDBj:3si2
• PDBsum: 3si2
• PubMed: 21671571
• UniProt: Q9CYK2|QPCT_MOUSE Glutaminyl-peptide cyclotransferase (Gene Name=Qpct)