eF-site ID 1s1t-B PDB Code 1s1t Chain B click to enlarge Title Crystal structure of L100I mutant HIV-1 reverse transcriptase in complex with UC-781 Classification TRANSFERASE Compound Reverse transcriptase Source Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) (POL_HV1H2) Sequence B:  PIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEK EGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKR TQDFWGIPHPAGIKKKKSVTVLDVGDAYFSVPLDEDFRKY TAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKI LEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQ HLLRWGLTELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKL NWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELA ENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQE PFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWG KTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVK LWYQLEKEPIVGAETF Description Functional site 1) chain B residue 356 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1000 source : AC1 2) chain B residue 359 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1000 source : AC1 3) chain B residue 238 type SITE sequence K description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 4) chain B residue 271 type SITE sequence Y description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 5) chain B residue 277 type SITE sequence R description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 6) chain B residue 66 type SITE sequence K description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA source Swiss-Prot : SWS_FT_FI4 7) chain B residue 235-252 type ZN_FING sequence HPDKWTVQPIVLPEKDSW description CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 256-273 type ZN_FING sequence DIQKLVGKLNWASQIYPG description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 358 type ACT_SITE sequence R description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150 source Swiss-Prot : SWS_FT_FI3 10) chain B residue 358 type catalytic sequence R description 175 source MCSA : MCSA1 11) chain B residue 359 type catalytic sequence G description 175 source MCSA : MCSA1 12) chain B residue 360 type catalytic sequence A description 175 source MCSA : MCSA1 13) chain B residue 333 type SITE sequence G description Cleavage; by viral protease => ECO:0000305|PubMed:15183348 source Swiss-Prot : SWS_FT_FI7 14) chain B residue 208 type SITE sequence H description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 285 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 16) chain B residue 432 type SITE sequence E description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5

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