1awr Summary

pdbe.org/1awr
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CYPA COMPLEXED WITH HAGPIA

The structure was published by Vajdos, F.F., Yoo, S., Houseweart, M., Sundquist, W.I., and Hill, C.P., in 1997 in a paper entitled "Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.58 Å and deposited in 1997.

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 PEPTIDE FROM THE HIV-1 CAPSID PROTEIN.

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 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
B CYCLOPHILIN A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
C CYCLOPHILIN A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
D CYCLOPHILIN A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
E CYCLOPHILIN A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
F CYCLOPHILIN A P62937 (2-165) (PPIA_HUMAN)search Homo sapienssearch 99% 164 100%
G PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%
H PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%
I PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%
J PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%
K PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%
L PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Not available
Not available Not available 6 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62937 (2 - 165) CYCLOPHILIN A Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F (P62937) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
G, H, I, J, K, L

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

Chain InterPro annotation
A, B, C, D, E, F 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
G, H, I, J, K, L