eF-site ID 1hmv-CDGH PDB Code 1hmv Chain C, D, G, H click to enlarge Title THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 Classification NUCLEOTIDYLTRANSFERASE Compound HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P66) Source Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) (POL_HV1B1) Sequence C:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA HKGIGGNEQVDKLVSA D:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY G:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA HKGIGGNEQVDKLVSA H:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY Description Functional site 1) chain C residue 443 type sequence D description BINDING SITE FOR RESIDUE MG D 501 source : AC2 2) chain C residue 478 type sequence E description BINDING SITE FOR RESIDUE MG D 501 source : AC2 3) chain C residue 498 type sequence D description BINDING SITE FOR RESIDUE MG D 501 source : AC2 4) chain G residue 443 type sequence D description BINDING SITE FOR RESIDUE MG H 501 source : AC4 5) chain G residue 478 type sequence E description BINDING SITE FOR RESIDUE MG H 501 source : AC4 6) chain G residue 498 type sequence D description BINDING SITE FOR RESIDUE MG H 501 source : AC4 7) chain D residue 244-261 type ZN_FING sequence IVLPEKDSWTVNDIQKLV description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI2 8) chain H residue 244-261 type ZN_FING sequence IVLPEKDSWTVNDIQKLV description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI2 9) chain D residue 358 type ACT_SITE sequence R description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029 source Swiss-Prot : SWS_FT_FI3 10) chain H residue 358 type ACT_SITE sequence R description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029 source Swiss-Prot : SWS_FT_FI3 11) chain D residue 54 type SITE sequence N description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 12) chain H residue 54 type SITE sequence N description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 13) chain D residue 273 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 14) chain D residue 333 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 15) chain H residue 273 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 16) chain H residue 333 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 17) chain C residue 220 type MOD_RES sequence K description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI10 18) chain C residue 242 type MOD_RES sequence Q description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI10 19) chain G residue 220 type MOD_RES sequence K description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI10 20) chain G residue 242 type MOD_RES sequence Q description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI10 21) chain G residue 273 type SITE sequence G description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI8 22) chain G residue 333 type SITE sequence G description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI8 23) chain D residue 242 type MOD_RES sequence Q description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI9 24) chain H residue 242 type MOD_RES sequence Q description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 source Swiss-Prot : SWS_FT_FI9 25) chain D residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 26) chain D residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 27) chain H residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 28) chain H residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 29) chain D residue 265 type SITE sequence N description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 30) chain H residue 265 type SITE sequence N description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 31) chain G residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 32) chain G residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6

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