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

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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 B:  TGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGF
DRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEA
IGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIH
ISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWM
TVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMQL
LEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDI
IYADGGAHTQLL
Description


Functional site

1) chain B
residue 14
type
sequence G
description binding site for residue 9JJ B 300
source : AC2

2) chain B
residue 15
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

3) chain B
residue 16
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

4) chain B
residue 20
type
sequence S
description binding site for residue 9JJ B 300
source : AC2

5) chain B
residue 21
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

6) chain B
residue 41
type
sequence F
description binding site for residue 9JJ B 300
source : AC2

7) chain B
residue 63
type
sequence L
description binding site for residue 9JJ B 300
source : AC2

8) chain B
residue 64
type
sequence D
description binding site for residue 9JJ B 300
source : AC2

9) chain B
residue 65
type
sequence V
description binding site for residue 9JJ B 300
source : AC2

10) chain B
residue 94
type
sequence S
description binding site for residue 9JJ B 300
source : AC2

11) chain B
residue 95
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

12) chain B
residue 96
type
sequence G
description binding site for residue 9JJ B 300
source : AC2

13) chain B
residue 122
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

14) chain B
residue 147
type
sequence M
description binding site for residue 9JJ B 300
source : AC2

15) chain B
residue 148
type
sequence D
description binding site for residue 9JJ B 300
source : AC2

16) chain B
residue 149
type
sequence F
description binding site for residue 9JJ B 300
source : AC2

17) chain B
residue 158
type
sequence Y
description binding site for residue 9JJ B 300
source : AC2

18) chain B
residue 161
type
sequence M
description binding site for residue 9JJ B 300
source : AC2

19) chain B
residue 165
type
sequence K
description binding site for residue 9JJ B 300
source : AC2

20) chain B
residue 192
type
sequence G
description binding site for residue 9JJ B 300
source : AC2

21) chain B
residue 193
type
sequence P
description binding site for residue 9JJ B 300
source : AC2

22) chain B
residue 194
type
sequence I
description binding site for residue 9JJ B 300
source : AC2

23) chain B
residue 196
type
sequence T
description binding site for residue 9JJ B 300
source : AC2

24) chain B
residue 198
type
sequence A
description binding site for residue 9JJ B 300
source : AC2

25) chain B
residue 199
type
sequence M
description binding site for residue 9JJ B 300
source : AC2

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

27) chain B
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

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

33) chain B
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

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


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