eF-site ID 7c2k-ABCD
PDB Code 7c2k
Chain A, B, C, D

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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
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 A
residue 545
type
sequence K
description binding site for Di-nucleotide F86 G 4 and G G 5
source : AC4
14) chain A
residue 623
type
sequence D
description binding site for Di-nucleotide F86 G 4 and G G 5
source : AC4
15) chain A
residue 682
type
sequence S
description binding site for Di-nucleotide F86 G 4 and G G 5
source : AC4
16) chain A
residue 759
type
sequence S
description binding site for Di-nucleotide F86 G 4 and G G 5
source : AC4
17) chain A
residue 814
type
sequence S
description binding site for Di-nucleotide F86 G 4 and G G 5
source : AC4
18) 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
19) 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
20) 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
21) 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
22) 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
23) 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
24) 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
25) 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
26) chain A
residue 590-601
type prosite
sequence GTSKFYGGWHNM
description LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM
source prosite : PS00213
27) chain A
residue 761
type SITE
sequence D
description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
source Swiss-Prot : SWS_FT_FI1
28) chain A
residue 209
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
source Swiss-Prot : SWS_FT_FI2
29) chain A
residue 218
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
source Swiss-Prot : SWS_FT_FI2

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