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Overview for MACiE Entry M0189

Version history

General Information

EC Number: 5.2.1.8 (A member of the Isomerases, cis-trans-Isomerases, cis-trans Isomerases (only sub-subclass identified to date))

Enzyme Name: peptidylprolyl isomerase

Biological Species: Homo sapiens (Human)

Catalytic Chain UniprotKB Accession Codes:

  • P62937 - Peptidyl-prolyl cis-trans isomerase A

Representative PDB Code: 1m9c - X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/HIV-1 CA N-TERMINAL DOMAIN (1-146) M-TYPE COMPLEX. (Resolution = 2.00 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

  • 1.10.375.10 - Human Immunodeficiency Virus Type 1 Capsid Protein

Display structure information

Overall Reaction:

Image of peptidylproline (omega=180)

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Image of peptidylproline (omega=0)

peptidylproline (omega=180)
C03798
CHEBI:50342
peptidylproline (omega=0)
C03633
CHEBI:30018

View similar reactions


Stepwise Description of the Reaction

Step 1The enzyme stabilises the transition state of the isomerisation of peptidylproline omega=180 to peptidylproline omega=0.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Arg 55 A Side Chain
Phe 60 A Side Chain
Gln 63 A Side Chain
Asn 102 A Main Chain Carbonyl
Main Chain Amide
Phe 113 A Side Chain
Leu 122 A Side Chain
His 126 A Side Chain

References

  1. B. R. Howard et al. (2003), Nat. Struct. Biol., 10, 475-481. Structural insights into the catalytic mechanism of cyclophilin A.
    Medline: 12730686
  2. P. K. Agarwal (2004), Proteins, 56, 449-463. Cis/trans isomerization in HIV-1 capsid protein catalyzed by cyclophilin A: insights from computational and theoretical studies.
    Medline: 15229879
  3. G. Li et al. (2003), J. Am. Chem. Soc., 125, 15028-15038. What is so special about Arg 55 in the catalysis of cyclophilin A? insights from hybrid QM/MM simulations.
    Medline: 14653737

Homologue information for M0189 (1m9c)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

GOA logo
platelet degranulation (biological process)
peptidyl-prolyl cis-trans isomerase activity (molecular function)
protein binding (molecular function)
extracellular region (cellular component)
nucleus (cellular component)
cytoplasm (cellular component)
cytosol (cellular component)
RNA-dependent DNA replication (biological process)
protein folding (biological process)
blood coagulation (biological process)
viral process (biological process)
isomerase activity (molecular function)
()
initiation of viral infection (biological process)
uncoating of virus (biological process)
platelet activation (biological process)
entry into host cell (biological process)
peptide binding (molecular function)
interspecies interaction between organisms (biological process)
regulation of viral genome replication (biological process)
virion binding (molecular function)
leukocyte migration (biological process)
unfolded protein binding (molecular function)
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