Structure of PDB 2pre Chain A

Receptor sequence
>2preA (length=208) Species: 52861 (Tabernaemontana divaricata) [Search protein sequence]
LPEQIDWRKKGAVTPVKNQGKCGSCWAFSTVSTVESINQIRTGNLISLSE
QQLVDCNKKNHGCKGGAFVYAYQYIIDNGGIDTEANYPYKAVQGPCRAAK
KVVRIDGYKGVPHCNENALKKAVASQPSVVAIDASSKQFQHYKSGIFSGP
CGTKLNHGVVIVGYWKDYWIVRNSWGRYWGEQGYIRMKRVGGCGLCGIAR
LPYYPTKA
3D structure
PDB2pre Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q19 C25 H157 N173
Catalytic site (residue number reindexed from 1) Q19 C25 H157 N173
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 E64 A Q19 G23 C25 H61 G65 N156 H157 Q19 G23 C25 H61 G65 N156 H157 PDBbind-CN: -logKd/Ki=6.65,IC50=225nM
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:2pre, PDBe:2pre, PDBj:2pre
PDBsum2pre
PubMed18167146
UniProtA8DS38|ERVC2_TABDI Ervatamin-C

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