eF-site ID 1bdm-AB
PDB Code 1bdm
Chain A, B

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Title THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A SINGLE SITE MUTANT (T189I) OF MALATE DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED ENZYMATIC ACTIVITY
Classification OXIDOREDUCTASE(NAD(A)-CHOH(D))
Compound MALATE DEHYDROGENASE
Source null (MDH_THETH)
Sequence A:  MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQL
LEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPDVAFKD
ADYALLVGAAPRLQVNGKIFTEQGRALAEVAKKDVKVLVV
GNPANTNALIAYKNAPGLNPRNFTAMTRLDHNRAKAQLAK
KTGTGVDRIRRMTVWGNHSSIMFPDLFHAEVDGRPALELV
DMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHI
RDWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDG
AYRVVEGLEINEFARKRMEITAQELLDEMEQVKALGLI
B:  MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQL
LEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPDVAFKD
ADYALLVGAAPRKAGMERRDLLQVNGKIFTEQGRALAEVA
KKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDH
NRAKAQLAKKTGTGVDRIRRMTVWGNHSSIMFPDLFHAEV
DGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAAS
AANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVY
SFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQ
VKALGLI
Description


Functional site

1) chain A
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

2) chain A
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

3) chain A
residue 14
type
sequence Q
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

4) chain A
residue 15
type
sequence I
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

5) chain A
residue 41
type
sequence E
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

6) chain A
residue 42
type
sequence I
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

7) chain A
residue 86
type
sequence V
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

8) chain A
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

9) chain A
residue 88
type
sequence A
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

10) chain A
residue 111
type
sequence Q
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

11) chain A
residue 128
type
sequence V
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

12) chain A
residue 129
type
sequence G
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

13) chain A
residue 130
type
sequence N
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

14) chain A
residue 154
type
sequence M
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

15) chain A
residue 186
type
sequence H
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

16) chain A
residue 245
type
sequence A
description BINDING SITE FOR RESIDUE NAX A 334
source : AC1

17) chain B
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

18) chain B
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

19) chain B
residue 14
type
sequence Q
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

20) chain B
residue 15
type
sequence I
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

21) chain B
residue 41
type
sequence E
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

22) chain B
residue 42
type
sequence I
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

23) chain B
residue 86
type
sequence V
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

24) chain B
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

25) chain B
residue 88
type
sequence A
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

26) chain B
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

27) chain B
residue 111
type
sequence Q
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

28) chain B
residue 128
type
sequence V
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

29) chain B
residue 129
type
sequence G
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

30) chain B
residue 130
type
sequence N
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

31) chain B
residue 154
type
sequence M
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

32) chain B
residue 186
type
sequence H
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

33) chain B
residue 245
type
sequence A
description BINDING SITE FOR RESIDUE NAX B 334
source : AC2

34) chain A
residue 186
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 186
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI1

36) chain A
residue 128
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 10
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 128
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 10
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 161
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

41) chain B
residue 91
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

42) chain B
residue 97
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

43) chain B
residue 104
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

44) chain B
residue 161
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

45) chain B
residue 130
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 91
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 104
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 130
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 111
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341
source Swiss-Prot : SWS_FT_FI4

50) chain A
residue 111
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341
source Swiss-Prot : SWS_FT_FI4

51) chain A
residue 154-166
type prosite
sequence MTRLDHNRAKAQL
description MDH Malate dehydrogenase active site signature. MTRLDhnRAkaqL
source prosite : PS00068


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