Structure of PDB 1ezu Chain D Binding Site BS01

Receptor Information
>1ezu Chain D (length=223) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGDEQFVNAAKIIKHPNFDRKTLNNNIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1ezu Chain D Residue 950 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ezu Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		N772 V775 L776 E777 E780
Binding residue
(residue number reindexed from 1)		N54 V57 L58 E59 E62
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H757 N802 Q892 G893 D894 S895 G896
Catalytic site (residue number reindexed from 1) H40 N84 Q174 G175 D176 S177 G178
Enzyme Commision number 3.4.21.4: trypsin.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007584 response to nutrient
GO:0007586 digestion
GO:0030574 collagen catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ezu, PDBe:1ezu, PDBj:1ezu
PDBsum1ezu
PubMed10843853
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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