1m9e Summary


X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A Complex.

The structure was published by Howard, B.R., Vajdos, F.F., Li, S., Sundquist, W.I., and Hill, C.P., in 2003 in a paper entitled "Structural insights into the catalytic mechanism of cyclophilin A" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.72 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Cyclophilin A and HIV-1 Capsid.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Cyclophilin A P62937 (1-164) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
B Cyclophilin A P62937 (1-164) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
C HIV-1 Capsid Q72497 (133-278) (Q72497_9HIV1)search Human immunodeficiency virus 1search < 90% 146 100%
D HIV-1 Capsid Q72497 (133-278) (Q72497_9HIV1)search Human immunodeficiency virus 1search < 90% 146 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P62937 (1 - 164) Cyclophilin A Homo sapiens
Q72497 (133 - 278) HIV-1 Capsid Human immunodeficiency virus 1

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P62937) Cyclophilin (peptidylprolyl isomerase)search Cyclophilin-likesearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
C, D Retrovirus capsid protein, N-terminal core domainsearch Human Immunodeficiency Virus Type 1 Capsid Proteinsearch gag gene protein p24 (core nucleocapsid protein)search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P62937) protein peptidyl-prolyl isomerizationsearch platelet degranulationsearch RNA-dependent DNA replicationsearch protein foldingsearch blood coagulationsearch viral processsearch viral life cyclesearch uncoating of virussearch virion assemblysearch viral release from host cellsearch platelet activationsearch entry into host cellsearch lipid particle organizationsearch regulation of viral genome replicationsearch positive regulation of viral genome replicationsearch positive regulation of protein secretionsearch leukocyte migrationsearch establishment of integrated proviral latencysearch peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch isomerase activitysearch peptide bindingsearch poly(A) RNA bindingsearch virion bindingsearch unfolded protein bindingsearch extracellular regionsearch extracellular spacesearch nucleussearch cytoplasmsearch cytosolsearch focal adhesionsearch membranesearch extracellular vesicular exosomesearch
C, D (Q72497) viral processsearch

Chain InterPro annotation
A, B Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainsearch Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved sitesearch Cyclophilin-type peptidyl-prolyl cis-trans isomerasesearch Cyclophilin-like domainsearch
C, D Retroviral nucleocapsid protein Gagsearch Retrovirus capsid, N-terminal domainsearch