eF-site ID 7c2k-ABCDFG PDB Code 7c2k Chain A, B, C, D, F, G click to enlarge Title COVID-19 RNA-dependent RNA polymerase pre-translocated catalytic complex Classification VIRAL PROTEIN/RNA Compound RNA-directed RNA polymerase Source (7C2K) Sequence A:  SADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYND KVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNY QHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLT KYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKK DWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAG IVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSL LMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERL KLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTV FPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVN LHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAA LTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHF FFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYF DCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMS YEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGV SICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHN MLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLAR KHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGT SSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYV RNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSD DAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCW TETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGA GCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADV FHLYLQYIRKLHDELTGHMLDMYSVMLDNTSRYWEPEFYE AMYTPHT B:  SEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCV PLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWE IQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRAN C:  PSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDI LLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLC D:  AAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLF TMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVI PDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEI SMDNSPNLAWPLIVTALRA F:  GGGAGCUCCUCCUGUGUCGU G:  ACGACACAGGXG Description Functional site 1) chain A residue 295 type sequence H description binding site for residue ZN A 1001 source : AC1 2) chain A residue 301 type sequence C description binding site for residue ZN A 1001 source : AC1 3) chain A residue 306 type sequence C description binding site for residue ZN A 1001 source : AC1 4) chain A residue 310 type sequence C description binding site for residue ZN A 1001 source : AC1 5) chain A residue 487 type sequence C description binding site for residue ZN A 1002 source : AC2 6) chain A residue 642 type sequence H description binding site for residue ZN A 1002 source : AC2 7) chain A residue 645 type sequence C description binding site for residue ZN A 1002 source : AC2 8) chain A residue 646 type sequence C description binding site for residue ZN A 1002 source : AC2 9) chain A residue 759 type sequence S description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 10) chain A residue 813 type sequence C description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 11) chain A residue 814 type sequence S description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 12) chain A residue 836 type sequence R description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 13) chain F residue -2 type sequence C description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 14) chain F residue -4 type sequence U description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 15) chain F residue -3 type sequence C description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 16) chain G residue 2 type sequence G description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 17) chain G residue 5 type sequence G description binding site for Di-nucleotide G G 3 and F86 G 4 source : AC3 18) chain A residue 545 type sequence K description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 19) chain A residue 623 type sequence D description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 20) chain A residue 682 type sequence S description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 21) chain A residue 759 type sequence S description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 22) chain A residue 814 type sequence S description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 23) chain F residue -3 type sequence C description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 24) chain F residue -5 type sequence C description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 25) chain F residue -4 type sequence U description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 26) chain G residue 3 type sequence G description binding site for Di-nucleotide F86 G 4 and G G 5 source : AC4 27) chain A residue 645 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 487 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI4 29) chain A residue 642 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI4 30) chain A residue 646 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI4 31) chain A residue 761 type SITE sequence D description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 209 type BINDING sequence N description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 33) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 34) chain A residue 295 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI3 35) chain A residue 301 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI3 36) chain A residue 306 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI3 37) chain A residue 310 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI3 38) chain A residue 590-601 type prosite sequence GTSKFYGGWHNM description LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM source prosite : PS00213

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