eF-site ID 6yyt-ABCDPQTU PDB Code 6yyt Chain A, B, C, D, P, Q, T, U click to enlarge Title Structure of replicating SARS-CoV-2 polymerase Classification VIRAL PROTEIN Compound nsp12 Source (6YYT) Sequence A:  VYRAFDIYNDKVAGFAKFLKFSNYQHEETIYNLLKDCPAV ARLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDY FNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAM RNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDS YYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFT EERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVL FSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHN QDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCF SVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVE LKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVV DKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYY DSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRART VAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYG GWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASL VLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVK PGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIA DKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMM ILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSE AKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSR ILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQE YADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYW EPEFYEAMYTPHT B:  FSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVA KSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTS AMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTA AKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSK IVQLSEISMDNSPNLAWPLIVTALRA C:  SKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDIL LAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCE D:  FSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVA KSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTS AMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTA AKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSK IVQLSEISMDNSPNLAWPLIVTALRA P:  CAUGCUACGCGUAG Q:  CAUGCUACGCGUAG T:  UGCUACGCGUAG U:  CAUGCUACGCGUAG Description Functional site 1) chain A residue 295 type sequence H description binding site for residue ZN A 2000 source : AC1 2) chain A residue 301 type sequence C description binding site for residue ZN A 2000 source : AC1 3) chain A residue 306 type sequence C description binding site for residue ZN A 2000 source : AC1 4) chain A residue 310 type sequence C description binding site for residue ZN A 2000 source : AC1 5) chain A residue 487 type sequence C description binding site for residue ZN A 2001 source : AC2 6) chain A residue 642 type sequence H description binding site for residue ZN A 2001 source : AC2 7) chain A residue 645 type sequence C description binding site for residue ZN A 2001 source : AC2 8) chain A residue 646 type sequence C description binding site for residue ZN A 2001 source : AC2 9) chain A residue 590-601 type prosite sequence GTSKFYGGWHNM description LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM source prosite : PS00213 10) chain A residue 761 type SITE sequence D description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 209 type BINDING sequence N description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 12) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 13) 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 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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

Display surface Download Links