eF-site ID 7bv2-ABC
PDB Code 7bv2
Chain A, B, C

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Title The nsp12-nsp7-nsp8 complex bound to the template-primer RNA and triphosphate form of Remdesivir(RTP)
Classification VIRAL PROTEIN
Compound RNA-directed RNA polymerase
Source (7BV2)
Sequence A:  VYRAFDIYNDKVAGFAKFLKETIYNLLKDCPAVAKHDRLT
KYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKK
DWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAG
IVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSL
LMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERL
KLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTV
FPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVN
LHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAA
LTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHF
FFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYF
DCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMS
YEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGV
SICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHN
MLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLAR
KHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGT
SSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYV
RNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSD
DAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCW
TETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGA
GCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADV
FHLYLQYIRKLHDELNTSRYWEPEFYEAMYTPHT
B:  DKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPL
NIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQ
QVVDADSKIVQLSEISMDNSPNLAWPLIVTALRA
C:  KMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILL
AKDTTEAFEKMVSLLSVLLSMQG
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 553
type
sequence R
description binding site for residue POP A 1003
source : AC3
10) chain A
residue 623
type
sequence D
description binding site for residue POP A 1003
source : AC3
11) chain A
residue 619
type
sequence Y
description binding site for residue MG A 1004
source : AC4
12) chain A
residue 760
type
sequence D
description binding site for residue MG A 1004
source : AC4
13) chain A
residue 761
type
sequence D
description binding site for residue MG A 1005
source : AC5
14) chain A
residue 555
type
sequence R
description binding site for residue F86 P 101
source : AC6
15) chain A
residue 623
type
sequence D
description binding site for residue F86 P 101
source : AC6
16) chain A
residue 682
type
sequence S
description binding site for residue F86 P 101
source : AC6
17) chain A
residue 687
type
sequence T
description binding site for residue F86 P 101
source : AC6
18) chain A
residue 691
type
sequence N
description binding site for residue F86 P 101
source : AC6
19) chain A
residue 760
type
sequence D
description binding site for residue F86 P 101
source : AC6
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
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 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
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 590-601
type prosite
sequence GTSKFYGGWHNM
description LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM
source prosite : PS00213
25) chain A
residue 761
type SITE
sequence D
description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
source Swiss-Prot : SWS_FT_FI1
26) chain A
residue 209
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
source Swiss-Prot : SWS_FT_FI2
27) chain A
residue 218
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
source Swiss-Prot : SWS_FT_FI2
28) 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
29) 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
30) 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
31) 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

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