Structure of PDB 2fo5 Chain D Binding Site BS01
Receptor Information
>2fo5 Chain D (length=224) Species:
4513
(Hordeum vulgare) [
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DLPPSVDWRQKGAVTGVKDQGKCGSCWAFSTVVSVEGINAIRTGSLVSLS
EQELIDCDTADNDGCQGGLMDNAFEYIKNNGGLITEAAYPYRAARGTCNV
ARAAQNSPVVVHIDGHQDVPANSEEDLARAVANQPVSVAVEASGKAFMFY
SEGVFTGECGTELDHGVAVVGYGVAEDGKAYWTVKNSWGPSWGEQGYIRV
EKDSGASGGLCGIAMEASYPVKTY
Ligand information
>2fo5 Chain H (length=3) Species:
66430
(Streptomyces roseus) [
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LLR
Receptor-Ligand Complex Structure
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PDB
2fo5
Heterologous Expression, Purification, Refolding, and Structural-Functional Characterization of EP-B2, a Self-Activating Barley Cysteine Endoprotease.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
G26 C28 G69 G70 L71 M72 D166
Binding residue
(residue number reindexed from 1)
G24 C26 G67 G68 L69 M70 D164
Enzymatic activity
Catalytic site (original residue number in PDB)
Q22 C28 H167 N188
Catalytic site (residue number reindexed from 1)
Q20 C26 H165 N186
Enzyme Commision number
3.4.22.-
Gene Ontology
Molecular Function
GO:0008234
cysteine-type peptidase activity
Biological Process
GO:0006508
proteolysis
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Molecular Function
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Biological Process
External links
PDB
RCSB:2fo5
,
PDBe:2fo5
,
PDBj:2fo5
PDBsum
2fo5
PubMed
16793521
UniProt
P25250
|CYSP2_HORVU Cysteine proteinase EP-B 2 (Gene Name=EPB2)
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