eF-site ID 2jc1-AB
PDB Code 2jc1
Chain A, B

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Title CRYSTAL STRUCTURE OF HEPATITIS C VIRUS POLYMERASE IN COMPLEX WITH INHIBITOR SB698223
Classification HYDROLASE
Compound RNA-DEPENDENT RNA-POLYMERASE
Source Hepatitis C virus (O39930_9HEPC)
Sequence A:  SMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYAT
TSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKA
KLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAVNHIH
SVWKDLLEDTVTPIDTTIMAKNEVFCVQRKPARLIVFPDL
GVRVCEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLV
NTWKSKKNPMGFSYDTRCFDSTVTENDIRVEESIYQCCDL
APEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVL
TTSCGNTLTCYLKASAACRAAKLQDCTMLVNGDDLVVICE
SAGVQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITS
CSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPV
NSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDC
QIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRV
ASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYL
FNWAVKTKLKLTPIPAWFVAGYSGGDIYH
B:  SMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYAT
TSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKA
KLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAVNHIH
SVWKDLLEDTVTPIDTTIMAKNEVFCVQRKPARLIVFPDL
GVRVCEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLV
NTWKSKKNPMGFSYDTRCFDSTVTENDIRVEESIYQCCDL
APEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVL
TTSCGNTLTCYLKASAACRAAKLQDCTMLVNGDDLVVICE
SAGVQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITS
CSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPV
NSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDC
QIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRV
ASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYL
FNWAVKTLTPIWFVAGYSGGDIYHS
Description (1)  RNA-DEPENDENT RNA-POLYMERASE


Functional site

1) chain A
residue 366
type
sequence C
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

2) chain A
residue 368
type
sequence S
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

3) chain A
residue 407
type
sequence S
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

4) chain A
residue 410
type
sequence G
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

5) chain A
residue 411
type
sequence N
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

6) chain A
residue 414
type
sequence M
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

7) chain A
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

8) chain A
residue 446
type
sequence Q
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

9) chain A
residue 447
type
sequence I
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

10) chain A
residue 448
type
sequence Y
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

11) chain A
residue 449
type
sequence G
description BINDING SITE FOR RESIDUE 698 A 600
source : AC1

12) chain B
residue 200
type
sequence R
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

13) chain B
residue 366
type
sequence C
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

14) chain B
residue 368
type
sequence S
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

15) chain B
residue 407
type
sequence S
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

16) chain B
residue 410
type
sequence G
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

17) chain B
residue 411
type
sequence N
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

18) chain B
residue 414
type
sequence M
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

19) chain B
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

20) chain B
residue 446
type
sequence Q
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

21) chain B
residue 448
type
sequence Y
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

22) chain B
residue 449
type
sequence G
description BINDING SITE FOR RESIDUE 698 B 600
source : AC2

23) chain A
residue 220
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 318
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 319
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 220
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 318
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 319
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 29
type MOD_RES
sequence S
description Phosphoserine; by host => ECO:0000250|UniProtKB:P26662
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 42
type MOD_RES
sequence S
description Phosphoserine; by host => ECO:0000250|UniProtKB:P26662
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 29
type MOD_RES
sequence S
description Phosphoserine; by host => ECO:0000250|UniProtKB:P26662
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 42
type MOD_RES
sequence S
description Phosphoserine; by host => ECO:0000250|UniProtKB:P26662
source Swiss-Prot : SWS_FT_FI2


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