PPIRE08637

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 P9
Peptide_Sequence PPPPPPPPP
Peptide_Length 9
Peptide_SMILES O=C(O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=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 892.07
Aliphatic_Index 0.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 1.00000
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 10
Number_of_Hydrogen_Bond_Donors 2
Topological_Polar_Surface_Area 211.81000
X_logP_energy -0.24900
Interaction Information
Affinity KD=9.8 uM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 4BTB
Type Inhibitor
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