eF-site ID 1hmv-ABEF PDB Code 1hmv Chain A, B, E, F 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 A:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA HKGIGGNEQVDKLVSA B:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY E:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA HKGIGGNEQVDKLVSA F:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY Description Functional site 1) chain A residue 443 type sequence D description BINDING SITE FOR RESIDUE MG B 501 source : AC1 2) chain A residue 478 type sequence E description BINDING SITE FOR RESIDUE MG B 501 source : AC1 3) chain A residue 498 type sequence D description BINDING SITE FOR RESIDUE MG B 501 source : AC1 4) chain E residue 443 type sequence D description BINDING SITE FOR RESIDUE MG F 501 source : AC3 5) chain E residue 478 type sequence E description BINDING SITE FOR RESIDUE MG F 501 source : AC3 6) chain E residue 498 type sequence D description BINDING SITE FOR RESIDUE MG F 501 source : AC3 7) chain A 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 8) chain A 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 9) chain E 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 10) chain E 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 11) chain B residue 244-261 type ZN_FING sequence IVLPEKDSWTVNDIQKLV description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI2 12) chain F residue 244-261 type ZN_FING sequence IVLPEKDSWTVNDIQKLV description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 source Swiss-Prot : SWS_FT_FI2 13) chain B 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 14) chain F 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 15) chain B 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 16) chain F 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 17) chain B residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 18) chain B residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 19) chain F residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 20) chain F residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 21) chain B residue 265 type SITE sequence N description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 22) chain F residue 265 type SITE sequence N description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 23) chain E residue 196 type SITE sequence G description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 24) chain E residue 210 type SITE sequence L description Cleavage; by viral protease => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 273 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 26) chain B residue 333 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 27) chain F residue 273 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 28) chain F residue 333 type SITE sequence G description Cleavage; by viral protease source Swiss-Prot : SWS_FT_FI7 29) chain E residue 273 type SITE sequence G description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI8 30) chain E residue 333 type SITE sequence G description Cleavage; by viral protease => ECO:0000269|PubMed:2476069 source Swiss-Prot : SWS_FT_FI8 31) chain B 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 32) chain F 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

Display surface Download Links