eF-site ID 4uon-AB
PDB Code 4uon
Chain A, B

click to enlarge
Title Crystal structure of C-terminal truncated (110-265) Aura virus capsid protease.
Classification HYDROLASE
Compound CAPSID PROTEASE
Source Aura virus (AURAV) (POLS_AURAV)
Sequence A:  HMALKFEADRTFAVKNEDGKIMGYAVAMEGKVIKPLHVKG
TIDHPALAKLKFTKSSSYDMEFAKLPTEMKSDAFGYTTEH
PEGFYNWHHGAVQFSGGRFTIPTGAGGPGDSGRPILDNSG
KVVAIVLGGANEGARTALSVVTWNKKGAAIKTTH
B:  ALKFEADRTFAVKNEDGKIMGYAVAMEGKVIKPLHVKGTI
DHPALAKLKFTKSSSYDMEFAKLPTEMKSDAFGYTTEHPE
GFYNWHHGAVQFSGGRFTIPTGAGGPGDSGRPILDNSGKV
VAIVLGGANEGARTALSVVTWNKKGAAIKTTH
Description


Functional site

1) chain A
residue -1
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 1262
source : AC1

2) chain A
residue 147
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 1263
source : AC2

3) chain A
residue 148
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 1263
source : AC2

4) chain A
residue 149
type
sequence I
description BINDING SITE FOR RESIDUE GOL A 1263
source : AC2

5) chain A
residue 159
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 1263
source : AC2

6) chain A
residue 168
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 1263
source : AC2

7) chain A
residue 213
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

8) chain A
residue 214
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

9) chain A
residue 217
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

10) chain A
residue 218
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

11) chain A
residue 235
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

12) chain A
residue 245
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 1264
source : AC3

13) chain B
residue 147
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

14) chain B
residue 148
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

15) chain B
residue 149
type
sequence I
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

16) chain B
residue 155
type
sequence A
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

17) chain B
residue 159
type
sequence F
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

18) chain B
residue 168
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 1262
source : AC4

19) chain B
residue 131
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

20) chain B
residue 196
type
sequence H
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

21) chain B
residue 213
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

22) chain B
residue 214
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

23) chain B
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

24) chain B
residue 217
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

25) chain B
residue 220
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 1263
source : AC5

26) chain B
residue 194
type
sequence W
description BINDING SITE FOR RESIDUE GOL B 1264
source : AC6

27) chain B
residue 214
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1264
source : AC6

28) chain B
residue 217
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 1264
source : AC6

29) chain B
residue 218
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 1264
source : AC6

30) chain B
residue 236
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 1264
source : AC6

31) chain A
residue 144
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 166
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 218
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 144
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 166
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 218
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 191
type SITE
sequence F
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 192
type SITE
sequence Y
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 225
type SITE
sequence N
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2

40) chain B
residue 191
type SITE
sequence F
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 192
type SITE
sequence Y
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 225
type SITE
sequence N
description Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
source Swiss-Prot : SWS_FT_FI2


Display surface

Download
Links