eF-site ID 5vrm-D
PDB Code 5vrm
Chain D

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Title CRYSTAL STRUCTURE OF THE INHA FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AN12855, EBSI 4333.
Classification OXIDOREDUCTASE
Compound Enoyl-[acyl-carrier-protein] reductase [NADH]
Source (INHA_MYCTO)
Sequence D:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD
RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI
GAGNKLDGVVHSIGFMPQPFFDAPYADVSKGIHISAYSYA
SMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSAL
ESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIEAGAQI
QLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTG
DIIYADGGAHTQLL
Description


Functional site

1) chain D
residue 14
type
sequence G
description binding site for residue 9JJ D 300
source : AC4

2) chain D
residue 15
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

3) chain D
residue 16
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

4) chain D
residue 20
type
sequence S
description binding site for residue 9JJ D 300
source : AC4

5) chain D
residue 21
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

6) chain D
residue 41
type
sequence F
description binding site for residue 9JJ D 300
source : AC4

7) chain D
residue 63
type
sequence L
description binding site for residue 9JJ D 300
source : AC4

8) chain D
residue 64
type
sequence D
description binding site for residue 9JJ D 300
source : AC4

9) chain D
residue 65
type
sequence V
description binding site for residue 9JJ D 300
source : AC4

10) chain D
residue 95
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

11) chain D
residue 96
type
sequence G
description binding site for residue 9JJ D 300
source : AC4

12) chain D
residue 97
type
sequence F
description binding site for residue 9JJ D 300
source : AC4

13) chain D
residue 98
type
sequence M
description binding site for residue 9JJ D 300
source : AC4

14) chain D
residue 99
type
sequence P
description binding site for residue 9JJ D 300
source : AC4

15) chain D
residue 100
type
sequence Q
description binding site for residue 9JJ D 300
source : AC4

16) chain D
residue 122
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

17) chain D
residue 147
type
sequence M
description binding site for residue 9JJ D 300
source : AC4

18) chain D
residue 148
type
sequence D
description binding site for residue 9JJ D 300
source : AC4

19) chain D
residue 157
type
sequence A
description binding site for residue 9JJ D 300
source : AC4

20) chain D
residue 158
type
sequence Y
description binding site for residue 9JJ D 300
source : AC4

21) chain D
residue 159
type
sequence N
description binding site for residue 9JJ D 300
source : AC4

22) chain D
residue 161
type
sequence M
description binding site for residue 9JJ D 300
source : AC4

23) chain D
residue 165
type
sequence K
description binding site for residue 9JJ D 300
source : AC4

24) chain D
residue 191
type
sequence A
description binding site for residue 9JJ D 300
source : AC4

25) chain D
residue 193
type
sequence P
description binding site for residue 9JJ D 300
source : AC4

26) chain D
residue 194
type
sequence I
description binding site for residue 9JJ D 300
source : AC4

27) chain D
residue 196
type
sequence T
description binding site for residue 9JJ D 300
source : AC4

28) chain D
residue 20
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
source Swiss-Prot : SWS_FT_FI1

29) chain D
residue 64
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
source Swiss-Prot : SWS_FT_FI1

30) chain D
residue 95
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
source Swiss-Prot : SWS_FT_FI1

31) chain D
residue 165
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
source Swiss-Prot : SWS_FT_FI1

32) chain D
residue 194
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
source Swiss-Prot : SWS_FT_FI1

33) chain D
residue 158
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10336454
source Swiss-Prot : SWS_FT_FI2

34) chain D
residue 149
type SITE
sequence F
description May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454
source Swiss-Prot : SWS_FT_FI3

35) chain D
residue 158
type SITE
sequence Y
description Transition state stabilizer => ECO:0000305|PubMed:10521269
source Swiss-Prot : SWS_FT_FI4

36) chain D
residue 266
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326
source Swiss-Prot : SWS_FT_FI5


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