PPIRE08633

Target Protein Information
Protein_Name Prolyl 4-hydroxylase subunit alpha-1
Protein_Sequence MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Organism_Source Homo sapiens
Functional_Classification Fe(II)/2-oxoglutarate (2OG)–dependent oxygenases(2OG-oxygenases)
Cellular_Localization Cytoplasm
Gene_Names P4HA1
UniProt_ID P13674
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name (PPG)3
Peptide_Sequence PPGPPGPPG
Peptide_Length 9
Peptide_SMILES O=C(O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 771.87
Aliphatic_Index 0.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 1.33333
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 10
Number_of_Hydrogen_Bond_Donors 5
Topological_Polar_Surface_Area 238.18000
X_logP_energy -2.87340
Interaction Information
Affinity KD=144 uM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 4BT9
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title The structural motifs for substrate binding and dimerization of the Alpha subunit of collagen prolyl 4-hydroxylase.
Release_Year 2013
PMID 24207127
DOI 10.1016/j.str.2013.09.005