Structure of PDB 2fo5 Chain A

Receptor sequence
>2fo5A (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.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A G26 C28 C67 Q68 G69 G70 L71 L165 D166 G24 C26 C65 Q66 G67 G68 L69 L163 D164
Gene Ontology
Molecular Function
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2fo5, PDBe:2fo5, PDBj:2fo5
PDBsum2fo5
PubMed16793521
UniProtP25250|CYSP2_HORVU Cysteine proteinase EP-B 2 (Gene Name=EPB2)

[Back to BioLiP]