3IXO

Crystal Structure of uncomplexed HIV_1 Protease Subtype A

Summary for 3IXO

• Entry DOI: 10.2210/pdb3ixo/pdb
• Descriptor: HIV-1 protease (2 entities in total)
• Functional Keywords: hiv-1 protease, subtype a, uncomplexed, aspartyl protease, hydrolase, multifunctional enzyme, nucleotidyltransferase, protease, rna-directed dna polymerase, transferase
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 21539.47

Authors

Robbins, A.,McKenna, R. (deposition date: 2009-09-04, release date: 2010-03-02, Last modification date: 2023-09-06)

Primary citation

Robbins, A.H.,Coman, R.M.,Bracho-Sanchez, E.,Fernandez, M.A.,Gilliland, C.T.,Li, M.,Agbandje-McKenna, M.,Wlodawer, A.,Dunn, B.M.,McKenna, R.
Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes.
Acta Crystallogr.,Sect.D, 66:233-242, 2010

PubMed Abstract: The crystal structure of the unbound form of HIV-1 subtype A protease (PR) has been determined to 1.7 A resolution and refined as a homodimer in the hexagonal space group P6(1) to an R(cryst) of 20.5%. The structure is similar in overall shape and fold to the previously determined subtype B, C and F PRs. The major differences lie in the conformation of the flap region. The flaps in the crystal structures of the unbound subtype B and C PRs, which were crystallized in tetragonal space groups, are either semi-open or wide open. In the present structure of subtype A PR the flaps are found in the closed position, a conformation that would be more anticipated in the structure of HIV protease complexed with an inhibitor. The amino-acid differences between the subtypes and their respective crystal space groups are discussed in terms of the differences in the flap conformations.

PubMed: 20179334
DOI: 10.1107/S0907444909054298

Experimental method

X-RAY DIFFRACTION (1.7 Å)