eF-site ID 1s1t-AB PDB Code 1s1t Chain A, 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 A:  SPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEME KEGKISKIGPENPYNTPVFAIKWRKLVDFRELNKRTQDFW EVQLGIPHPAGIKKKKSVTVLDVGDAYFSVPLDEDFRKYT AFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKIL EPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQH LLRWGLTTPKKHQKEPPFLWMGYELHPDKWTVQPIVLPEK DSWTVNDIQKLVGKLNWASQIYPGIKVRQLXKLLRGTKAL TEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEI QKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLT EAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQAT WIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRE TKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDS GLEVNIVTDSQYALGIIQAQPDQSESELVNQIIEQLIKKE KVYLAWVPAHKGIG B:  PIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEK EGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKR TQDFWGIPHPAGIKKKKSVTVLDVGDAYFSVPLDEDFRKY TAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKI LEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQ HLLRWGLTELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKL NWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELA ENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQE PFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWG KTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVK LWYQLEKEPIVGAETF Description Functional site 1) chain A residue 447 type sequence N description BINDING SITE FOR RESIDUE PO4 B 1000 source : AC1 2) chain B residue 356 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1000 source : AC1 3) chain B residue 359 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1000 source : AC1 4) chain A residue 183 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 2001 source : AC2 5) chain A residue 229 type sequence W description BINDING SITE FOR RESIDUE PO4 A 2001 source : AC2 6) chain A residue 230 type sequence M description BINDING SITE FOR RESIDUE PO4 A 2001 source : AC2 7) chain A residue 101 type sequence K description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 8) chain A residue 103 type sequence K description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 9) chain A residue 179 type sequence V description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 10) chain A residue 181 type sequence Y description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 11) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 12) chain A residue 190 type sequence G description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 13) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 14) chain A residue 229 type sequence W description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 15) chain A residue 234 type sequence L description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 16) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE UC1 A 999 source : AC3 17) chain B residue 358 type catalytic sequence R description 175 source MCSA : MCSA1 18) chain B residue 359 type catalytic sequence G description 175 source MCSA : MCSA1 19) chain B residue 360 type catalytic sequence A description 175 source MCSA : MCSA1 20) 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 21) 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 22) 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 23) 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 24) chain B residue 208 type SITE sequence H description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 285 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 432 type SITE sequence E description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 238 type SITE sequence K description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 271 type SITE sequence Y description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 277 type SITE sequence R description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 432 type SITE sequence E description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 333 type SITE sequence G description Cleavage; by viral protease => ECO:0000305|PubMed:15183348 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 271 type SITE sequence Y description Cleavage; by viral protease => ECO:0000305|PubMed:15183348 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 277 type SITE sequence R description Cleavage; by viral protease => ECO:0000305|PubMed:15183348 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 333 type SITE sequence G description Cleavage; by viral protease => ECO:0000305|PubMed:15183348 source Swiss-Prot : SWS_FT_FI8

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