Structure of PDB 1ym0 Chain A Binding Site BS01
Receptor Information
>1ym0 Chain A (length=238) Species:
6396
(Eisenia fetida) [
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IVGGIEARPYEFPWQVSVRRKSSDSHFCGGSIINDRWVVCAAHCMQGEAP
ALVSLVVGEHDSSAASTVRQTHDVDSIFVNENYDPATLENDVSVIKTAVA
ITFDINVGPICAPDPANDYVYRKSQCSGWGTINSGGVCCPAVLRYVTLNI
TTNAFCDAVYTSDTIYDDMICATDNTGMTDRDSCQGDSGGPLSVKDGSGI
FSLVGIVSWGIGCASGYPGVYSRVGFHAGWITDTITNN
Ligand information
>1ym0 Chain B (length=27) Species:
6396
(Eisenia fetida) [
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QPPVWYPGGQCGVSQYSDAGDMELPPG
Receptor-Ligand Complex Structure
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PDB
1ym0
Crystal structure of earthworm fibrinolytic enzyme component B: a novel, glycosylated two-chained trypsin.
Resolution
2.06 Å
Binding residue
(original residue number in PDB)
R23 P24 E26 W29 I47 N48 F114 I116 P120 I121 C122 A123 P124 D125 K135 Y157 T159 L160 N186 R188 K202 I206 F207 I238 T239
Binding residue
(residue number reindexed from 1)
R8 P9 E11 W14 I33 N34 F103 I105 P109 I110 C111 A112 P113 D114 K123 Y145 T147 L148 N175 R181 K195 I200 F201 I231 T232
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
PDBsum
1ym0
PubMed
15826663
UniProt
Q3HR18
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