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BioLiP

Structure of PDB 3liz Chain A Binding Site BS03

Receptor Information
>3liz Chain A (length=329) Species: 6973 (Blattella germanica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIVPLYKLVHVFINTQYAGITKIGNQNFLTVFDSTSCNVVVASQECVGGA
CVCPNLQKYEKLKPKYISDGNVQVKFFDTGSAVGRGIEDSLTISQLTTSQ
QDIVLADELSQEVCILSADVVVGIAAPGCPNALKGKTVLENFVEENLIAP
VFSIHHARFQDGEHFGEIIFGGSDWKYVDGEFTYVPLVGDDSWKFRLDGV
KIGDTTVAPAGTQAIIDTSKAIIVGPKAYVNPINEAIGCVVEKTTTRRIC
KLDCSKIPSLPDVTFVINGRNFNISSQYYIQQNGNLCYSGFQPCGHSDHF
FIGDFFVDHYYSEFNWENKTMGFGRSVES
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain3liz Chain A Residue 336 [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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PDB3liz Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D297 H298
Binding residue
(residue number reindexed from 1)		D298 H299
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 V39 F75 D215 K218
Catalytic site (residue number reindexed from 1) D33 S36 N38 V40 F76 D217 K220
Enzyme Commision number 3.4.23.-
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3liz, PDBe:3liz, PDBj:3liz
PDBsum3liz
PubMed21789239
UniProtP54958|ASP2_BLAGE Aspartic protease Bla g 2

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