PPIRE08631

Target Protein Information
Protein_Name Prolyl 4-hydroxylase subunit alpha-2
Protein_Sequence MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
Organism_Source Homo sapiens
Functional_Classification prolyl 4-hydroxylase
Cellular_Localization Extracellular
Gene_Names P4HA2
UniProt_ID O15460
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name PPG-PAG-PPG
Peptide_Sequence PPGPAGPPG
Peptide_Length 9
Peptide_SMILES C[C@H](NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)NCC(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 745.83
Aliphatic_Index 11.11111
Aromaticity 0.00000
Average_Rotatable_Bonds 1.44444
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 10
Number_of_Hydrogen_Bond_Donors 6
Topological_Polar_Surface_Area 246.97000
X_logP_energy -3.35970
Interaction Information
Affinity KD=19.7 uM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 6EVN
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif.
Release_Year 2018
PMID 30168208
DOI 10.1002/pro.3450