1HAR
2.2 ANGSTROMS RESOLUTION STRUCTURE OF THE AMINO-TERMINAL HALF OF HIV-1 REVERSE TRANSCRIPTASE (FINGERS AND PALM SUBDOMAINS)
Summary for 1HAR
| Entry DOI | 10.2210/pdb1har/pdb |
| Descriptor | HIV-1 REVERSE TRANSCRIPTASE (FINGERS AND PALM SUBDOMAINS) (2 entities in total) |
| Functional Keywords | reverse transcriptase, viral protein, transferase, dna polymerase, fingers-palm subdomains, n-terminal half |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 24261.10 |
| Authors | Unge, T.,Knight, S.,Strandberg, B. (deposition date: 1994-10-28, release date: 1995-04-20, Last modification date: 2024-02-07) |
| Primary citation | Unge, T.,Knight, S.,Bhikhabhai, R.,Lovgren, S.,Dauter, Z.,Wilson, K.,Strandberg, B. 2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains). Structure, 2:953-961, 1994 Cited by PubMed Abstract: HIV-1 reverse transcriptase (RT) catalyzes the transformation of single-stranded viral RNA into double-stranded DNA, which is integrated into host cell chromosomes. The molecule is a heterodimer of two subunits, p51 and p66. The amino acid sequence of p51 is identical to the sequence of the amino-terminal subdomains of p66. Earlier crystallographic studies indicate that the RT molecule is flexible, which may explain the difficulty in obtaining high-resolution data for the intact protein. We have therefore determined the structure of a fragment of RT (RT216), which contains only the amino-terminal half of the RT molecule ('finger' and 'palm' subdomains). PubMed: 7532533DOI: 10.1016/S0969-2126(94)00097-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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