Structure of PDB 1ym0 Chain A Binding Site BS02

Receptor Information
>1ym0 Chain A (length=238) Species: 6396 (Eisenia fetida) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGIEARPYEFPWQVSVRRKSSDSHFCGGSIINDRWVVCAAHCMQGEAP
ALVSLVVGEHDSSAASTVRQTHDVDSIFVNENYDPATLENDVSVIKTAVA
ITFDINVGPICAPDPANDYVYRKSQCSGWGTINSGGVCCPAVLRYVTLNI
TTNAFCDAVYTSDTIYDDMICATDNTGMTDRDSCQGDSGGPLSVKDGSGI
FSLVGIVSWGIGCASGYPGVYSRVGFHAGWITDTITNN
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1ym0 Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ym0 Crystal structure of earthworm fibrinolytic enzyme component B: a novel, glycosylated two-chained trypsin.
Resolution2.06 Å
Binding residue
(original residue number in PDB)		D169 Y172 D174A
Binding residue
(residue number reindexed from 1)		D157 Y160 D163
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H43 D91 Q185 G186 D187 S188 G189
Enzyme Commision number 3.4.21.-
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1ym0, PDBe:1ym0, PDBj:1ym0
PDBsum1ym0
PubMed15826663
UniProtQ3HR18

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