eF-site ID 4z7y-ABCDEF
PDB Code 4z7y
Chain A, B, C, D, E, F

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Title diphosphomevalonate decarboxylase from the Sulfolobus solfataricus, space group P21
Classification LYASE
Compound Diphosphomevalonate decarboxylase
Source (DMD_SULSO)
Sequence A:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
B:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
C:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
D:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
E:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
F:  LKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDD
QLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFK
KIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNEL
LELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDG
EDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRS
AETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRH
SNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFD
AGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKV
LSRE
Description


Functional site

1) chain A
residue 148
type
sequence G
description binding site for residue SO4 A 401
source : AC1

2) chain A
residue 149
type
sequence G
description binding site for residue SO4 A 401
source : AC1

3) chain A
residue 168
type
sequence Q
description binding site for residue SO4 A 401
source : AC1

4) chain A
residue 172
type
sequence H
description binding site for residue SO4 A 401
source : AC1

5) chain A
residue 317
type
sequence D
description binding site for residue SO4 A 401
source : AC1

6) chain A
residue 318
type
sequence G
description binding site for residue SO4 A 401
source : AC1

7) chain B
residue 148
type
sequence G
description binding site for residue SO4 B 401
source : AC2

8) chain B
residue 149
type
sequence G
description binding site for residue SO4 B 401
source : AC2

9) chain B
residue 168
type
sequence Q
description binding site for residue SO4 B 401
source : AC2

10) chain B
residue 171
type
sequence R
description binding site for residue SO4 B 401
source : AC2

11) chain B
residue 172
type
sequence H
description binding site for residue SO4 B 401
source : AC2

12) chain B
residue 317
type
sequence D
description binding site for residue SO4 B 401
source : AC2

13) chain B
residue 318
type
sequence G
description binding site for residue SO4 B 401
source : AC2

14) chain C
residue 148
type
sequence G
description binding site for residue SO4 C 401
source : AC3

15) chain C
residue 149
type
sequence G
description binding site for residue SO4 C 401
source : AC3

16) chain C
residue 168
type
sequence Q
description binding site for residue SO4 C 401
source : AC3

17) chain C
residue 171
type
sequence R
description binding site for residue SO4 C 401
source : AC3

18) chain C
residue 172
type
sequence H
description binding site for residue SO4 C 401
source : AC3

19) chain D
residue 148
type
sequence G
description binding site for residue SO4 D 401
source : AC4

20) chain D
residue 149
type
sequence G
description binding site for residue SO4 D 401
source : AC4

21) chain D
residue 168
type
sequence Q
description binding site for residue SO4 D 401
source : AC4

22) chain D
residue 172
type
sequence H
description binding site for residue SO4 D 401
source : AC4

23) chain D
residue 317
type
sequence D
description binding site for residue SO4 D 401
source : AC4

24) chain D
residue 318
type
sequence G
description binding site for residue SO4 D 401
source : AC4

25) chain E
residue 148
type
sequence G
description binding site for residue SO4 E 401
source : AC5

26) chain E
residue 149
type
sequence G
description binding site for residue SO4 E 401
source : AC5

27) chain E
residue 168
type
sequence Q
description binding site for residue SO4 E 401
source : AC5

28) chain E
residue 172
type
sequence H
description binding site for residue SO4 E 401
source : AC5

29) chain E
residue 317
type
sequence D
description binding site for residue SO4 E 401
source : AC5

30) chain E
residue 318
type
sequence G
description binding site for residue SO4 E 401
source : AC5

31) chain F
residue 148
type
sequence G
description binding site for residue SO4 F 401
source : AC6

32) chain F
residue 168
type
sequence Q
description binding site for residue SO4 F 401
source : AC6

33) chain F
residue 171
type
sequence R
description binding site for residue SO4 F 401
source : AC6

34) chain F
residue 172
type
sequence H
description binding site for residue SO4 F 401
source : AC6

35) chain F
residue 317
type
sequence D
description binding site for residue SO4 F 401
source : AC6

36) chain F
residue 318
type
sequence G
description binding site for residue SO4 F 401
source : AC6

37) chain A
residue 121-128
type prosite
sequence LLELNLKS
description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLELNLKS
source prosite : PS00867

38) chain A
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

39) chain D
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

40) chain D
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

41) chain D
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

42) chain E
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

43) chain E
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

44) chain E
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

45) chain F
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

46) chain F
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

47) chain F
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

48) chain A
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

49) chain A
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

50) chain B
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

51) chain B
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

52) chain B
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

53) chain C
residue 18
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

54) chain C
residue 75
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1

55) chain C
residue 139
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:O23722
source Swiss-Prot : SWS_FT_FI1


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