Structure of PDB 2fo5 Chain D

Receptor sequence
>2fo5D (length=224) Species: 4513 (Hordeum vulgare) [Search protein sequence]
DLPPSVDWRQKGAVTGVKDQGKCGSCWAFSTVVSVEGINAIRTGSLVSLS
EQELIDCDTADNDGCQGGLMDNAFEYIKNNGGLITEAAYPYRAARGTCNV
ARAAQNSPVVVHIDGHQDVPANSEEDLARAVANQPVSVAVEASGKAFMFY
SEGVFTGECGTELDHGVAVVGYGVAEDGKAYWTVKNSWGPSWGEQGYIRV
EKDSGASGGLCGIAMEASYPVKTY
3D structure
PDB2fo5 Heterologous Expression, Purification, Refolding, and Structural-Functional Characterization of EP-B2, a Self-Activating Barley Cysteine Endoprotease.
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.-
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 D G26 C28 G69 G70 L71 M72 D166 G24 C26 G67 G68 L69 M70 D164
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
PDBsum2fo5
PubMed16793521
UniProtP25250|CYSP2_HORVU Cysteine proteinase EP-B 2 (Gene Name=EPB2)

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