Structure of PDB 1ym0 Chain A

Receptor sequence

>1ym0A (length=238) Species: 6396 (Eisenia fetida)

IVGGIEARPYEFPWQVSVRRKSSDSHFCGGSIINDRWVVCAAHCMQGEAP
ALVSLVVGEHDSSAASTVRQTHDVDSIFVNENYDPATLENDVSVIKTAVA
ITFDINVGPICAPDPANDYVYRKSQCSGWGTINSGGVCCPAVLRYVTLNI
TTNAFCDAVYTSDTIYDDMICATDNTGMTDRDSCQGDSGGPLSVKDGSGI
FSLVGIVSWGIGCASGYPGVYSRVGFHAGWITDTITNN

3D structure

• PDB: 1ym0 Crystal structure of earthworm fibrinolytic enzyme component B: a novel, glycosylated two-chained trypsin.
• Chain: A
• Resolution: 2.06 Å

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.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	A	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	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
BS02	MG	A	D169 Y172 D174A	D157 Y160 D163

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

External links

• PDB: RCSB:1ym0, PDBe:1ym0, PDBj:1ym0
• PDBsum: 1ym0
• PubMed: 15826663
• UniProt: Q3HR18