eF-site ID 1bdm-B
PDB Code 1bdm
Chain 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 Thermus thermophilus (MDH_THETH)
Sequence B:  MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQL
LEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPDVAFKD
ADYALLVGAAPRKAGMERRDLLQVNGKIFTEQGRALAEVA
KKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDH
NRAKAQLAKKTGTGVDRIRRMTVWGNHSSIMFPDLFHAEV
DGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAAS
AANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVY
SFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQ
VKALGLI
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

19) 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

20) 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

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

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

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

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

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

26) 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


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