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3HVT

STRUCTURAL BASIS OF ASYMMETRY IN THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE HETERODIMER

Replaces:  2HVTReplaces:  1HVT
Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003964molecular_functionRNA-directed DNA polymerase activity
A0004523molecular_functionRNA-DNA hybrid ribonuclease activity
A0006278biological_processRNA-templated DNA biosynthetic process
B0003964molecular_functionRNA-directed DNA polymerase activity
B0006278biological_processRNA-templated DNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NVP A 557
ChainResidue
ALEU100
ATYR319
ALYS101
AVAL106
ATYR181
ATYR188
APHE227
ATRP229
ALEU234
APRO236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BVAL111
BASP186
BLEU187

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
BPRO1
ALEU479
ASER499
ALYS550

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization
ChainResidueDetails
BTRP402
BGLU415

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Essential for RT p66/p51 heterodimerization
ChainResidueDetails
ATRP402
AGLU415

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by viral protease; partial
ChainResidueDetails
ATYR441

218853

PDB entries from 2024-04-24

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