Structure of PDB 5vjv Chain A Binding Site BS03

Receptor Information

>5vjv Chain A (length=298) Species: 3702 (Arabidopsis thaliana)

KPRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGP
ETRKVIDFLISLPEKHPDQTHVFLAGNHDFAFSGFLGLLPRPSDGSDLKD
TWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKAAYKGSIYDAGSTFE
SYGVPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIA
VHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSGRKNVWDIPQELDDKHTV
VVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLSS

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 5vjv Chain A Residue 403

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5vjv Structural basis for the preference of the Arabidopsis thalianaphosphatase RLPH2 for tyrosine-phosphorylated substrates.
• Resolution: 1.95 Å
• Binding residue (original residue number in PDB): D13 H15 D47
• Binding residue (residue number reindexed from 1): D10 H12 D44
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.1.3.48: protein-tyrosine-phosphatase.

Gene Ontology

Molecular Function

• GO:0004721 phosphoprotein phosphatase activity
• GO:0004722 protein serine/threonine phosphatase activity
• GO:0004725 protein tyrosine phosphatase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0035335 peptidyl-tyrosine dephosphorylation
• GO:0035970 peptidyl-threonine dephosphorylation
• GO:0070262 peptidyl-serine dephosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:5vjv, PDBe:5vjv, PDBj:5vjv
• PDBsum: 5vjv
• PubMed: 29615518
• UniProt: Q9SR62|RLPH2_ARATH Tyrosine-protein phosphatase RLPH2 (Gene Name=RLPH2)