eF-site ID 1jqv-A
PDB Code 1jqv
Chain A

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Title The K213E mutant of Lactococcus lactis Dihydroorotate dehydrogenase A
Classification OXIDOREDUCTASE
Compound Dihydroorotate dehydrogenase A
Source null (PYRDA_LACLC)
Sequence A:  MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAY
ITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYL
DYVLKNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDF
SGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKP
LGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLF
IDPEAESVVIKPEDGFGGIGGAYIKPTALANVRAFYTRLK
PEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPA
IFDRIIKELEEIMNQKGYQSIADFHGKLKSL
Description


Functional site

1) chain A
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE MG A 314
source : AC1

2) chain A
residue 35
type
sequence S
description BINDING SITE FOR RESIDUE MG A 314
source : AC1

3) chain A
residue 18
type
sequence A
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

4) chain A
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

5) chain A
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

6) chain A
residue 43
type
sequence K
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

7) chain A
residue 44
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

8) chain A
residue 58
type
sequence Y
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

9) chain A
residue 67
type
sequence N
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

10) chain A
residue 69
type
sequence M
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

11) chain A
residue 127
type
sequence N
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

12) chain A
residue 164
type
sequence K
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

13) chain A
residue 192
type
sequence V
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

14) chain A
residue 193
type
sequence N
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

15) chain A
residue 221
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

16) chain A
residue 248
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

17) chain A
residue 249
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

18) chain A
residue 250
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

19) chain A
residue 271
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

20) chain A
residue 272
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 1312
source : AC3

21) chain A
residue 43
type
sequence K
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

22) chain A
residue 67
type
sequence N
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

23) chain A
residue 69
type
sequence M
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

24) chain A
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

25) chain A
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

26) chain A
residue 127
type
sequence N
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

27) chain A
residue 193
type
sequence N
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

28) chain A
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE ORO A 1313
source : AC4

29) chain A
residue 213
type
sequence E
description BINDING SITE FOR RESIDUE ACY A 1001
source : AC7

30) chain A
residue 216
type
sequence F
description BINDING SITE FOR RESIDUE ACY A 1001
source : AC7

31) chain A
residue 238
type
sequence R
description BINDING SITE FOR RESIDUE ACY B 1003
source : AC9

32) chain A
residue 129
type
sequence S
description BINDING SITE FOR RESIDUE ACY A 1004
source : BC1

33) chain A
residue 193
type
sequence N
description BINDING SITE FOR RESIDUE ACY A 1004
source : BC1

34) chain A
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE ACY A 1004
source : BC1

35) chain A
residue 196
type
sequence G
description BINDING SITE FOR RESIDUE ACY A 1004
source : BC1

36) chain A
residue 218
type
sequence G
description BINDING SITE FOR RESIDUE ACY A 1004
source : BC1

37) chain A
residue 43
type catalytic
sequence K
description 892
source MCSA : MCSA1

38) chain A
residue 130
type catalytic
sequence C
description 892
source MCSA : MCSA1

39) chain A
residue 130
type ACT_SITE
sequence C
description Nucleophile
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 67
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 127
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

42) chain A
residue 193
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 43
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 38-57
type prosite
sequence GAYITKSSTLEKREGNPLPR
description DHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GayitKSSTlekReGNplPR
source prosite : PS00911

45) chain A
residue 245-265
type prosite
sequence IIGTGGIETGQDAFEHLLCGA
description DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGtGGIeTgqdAfeHLlCGA
source prosite : PS00912

46) chain A
residue 192
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 221
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 249
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 271
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 19
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 164
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329
source Swiss-Prot : SWS_FT_FI2


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