eF-site ID 6xqb-ABCDEF PDB Code 6xqb Chain A, B, C, D, E, F click to enlarge Title SARS-CoV-2 RdRp/RNA complex Classification VIRAL PROTEIN, TRANSFERASE/HYDROLASE Compound RNA-directed RNA polymerase Source (6XQB) Sequence A:  VYRAFDIYVAGFAKFLKRLTKYTMADLVYALRHFDEGNCD TLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGE RVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFG DFIQTGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKP YIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDD RCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVST GYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAAS GNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAV SKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMC DIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGF PFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNL KYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRG ATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDR AMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLS EMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANV NALLSTIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAY LRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYY QNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVY LPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYP LTKHPNQEYADVFHLYLQYIRKLHDELMLTNDNTSRYWEP E B:  DKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPL NIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQ QVVDADSKIVQLSEISMDNSPNLAWPLIVTALRA C:  KMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILL AKDTTEAFEKMVSLLSVLLSMQ D:  TSAMQTMLFTMLRKLDNDALNNIINNARDGC E:  GGGCCCA F:  GUGGGCCC 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 302 type sequence L description binding site for residue ZN A 1001 source : AC1 4) chain A residue 306 type sequence C description binding site for residue ZN A 1001 source : AC1 5) chain A residue 310 type sequence C description binding site for residue ZN A 1001 source : AC1 6) chain A residue 487 type sequence C description binding site for residue ZN A 1002 source : AC2 7) chain A residue 642 type sequence H description binding site for residue ZN A 1002 source : AC2 8) chain A residue 645 type sequence C description binding site for residue ZN A 1002 source : AC2 9) chain A residue 646 type sequence C description binding site for residue ZN A 1002 source : AC2 10) chain A residue 617 type sequence W description binding site for residue MG A 1003 source : AC3 11) chain A residue 761 type sequence D description binding site for residue MG A 1003 source : AC3 12) chain A residue 811 type sequence E description binding site for residue MG A 1003 source : AC3 13) 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 14) chain A residue 209 type BINDING sequence N description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 15) chain A residue 218 type BINDING sequence D description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ source Swiss-Prot : SWS_FT_FI2 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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 23) chain A residue 590-601 type prosite sequence GTSKFYGGWHNM description LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM source prosite : PS00213

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