eF-site ID 6yyt-ABCDPQTU
PDB Code 6yyt
Chain A, B, C, D, P, Q, T, U

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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


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