eF-site ID 4u0k-A
PDB Code 4u0k
Chain A

click to enlarge
Title Crystal structure of Mycobacterium tuberculosis enoyl reductase complexed with N-(5-chloro-2-methylphenyl)-1-cyclohexyl-5-oxopyrrolidine-3-carboxamide
Classification OXIDOREDUCTASE
Compound Enoyl-[acyl-carrier-protein] reductase [NADH]
Source (INHA_MYCTU)
Sequence A:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD
RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI
GAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHI
SAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMT
VAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAI
VGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTV
CALLSDWLPATTGDIIYADGGAHTQLL
Description


Functional site

1) chain A
residue 14
type
sequence G
description binding site for residue NAD A 500
source : AC1

2) chain A
residue 15
type
sequence I
description binding site for residue NAD A 500
source : AC1

3) chain A
residue 16
type
sequence I
description binding site for residue NAD A 500
source : AC1

4) chain A
residue 20
type
sequence S
description binding site for residue NAD A 500
source : AC1

5) chain A
residue 21
type
sequence I
description binding site for residue NAD A 500
source : AC1

6) chain A
residue 41
type
sequence F
description binding site for residue NAD A 500
source : AC1

7) chain A
residue 63
type
sequence L
description binding site for residue NAD A 500
source : AC1

8) chain A
residue 64
type
sequence D
description binding site for residue NAD A 500
source : AC1

9) chain A
residue 65
type
sequence V
description binding site for residue NAD A 500
source : AC1

10) chain A
residue 94
type
sequence S
description binding site for residue NAD A 500
source : AC1

11) chain A
residue 95
type
sequence I
description binding site for residue NAD A 500
source : AC1

12) chain A
residue 96
type
sequence G
description binding site for residue NAD A 500
source : AC1

13) chain A
residue 122
type
sequence I
description binding site for residue NAD A 500
source : AC1

14) chain A
residue 147
type
sequence M
description binding site for residue NAD A 500
source : AC1

15) chain A
residue 148
type
sequence D
description binding site for residue NAD A 500
source : AC1

16) chain A
residue 149
type
sequence F
description binding site for residue NAD A 500
source : AC1

17) chain A
residue 165
type
sequence K
description binding site for residue NAD A 500
source : AC1

18) chain A
residue 192
type
sequence G
description binding site for residue NAD A 500
source : AC1

19) chain A
residue 193
type
sequence P
description binding site for residue NAD A 500
source : AC1

20) chain A
residue 194
type
sequence I
description binding site for residue NAD A 500
source : AC1

21) chain A
residue 196
type
sequence T
description binding site for residue NAD A 500
source : AC1

22) chain A
residue 96
type
sequence G
description binding site for residue 744 A 501
source : AC2

23) chain A
residue 103
type
sequence M
description binding site for residue 744 A 501
source : AC2

24) chain A
residue 149
type
sequence F
description binding site for residue 744 A 501
source : AC2

25) chain A
residue 156
type
sequence P
description binding site for residue 744 A 501
source : AC2

26) chain A
residue 157
type
sequence A
description binding site for residue 744 A 501
source : AC2

27) chain A
residue 158
type
sequence Y
description binding site for residue 744 A 501
source : AC2

28) chain A
residue 161
type
sequence M
description binding site for residue 744 A 501
source : AC2

29) chain A
residue 199
type
sequence M
description binding site for residue 744 A 501
source : AC2

30) chain A
residue 215
type
sequence I
description binding site for residue 744 A 501
source : AC2

31) chain A
residue 218
type
sequence L
description binding site for residue 744 A 501
source : AC2

32) chain A
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

33) chain A
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

34) chain A
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

35) chain A
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

36) chain A
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

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

38) chain A
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

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

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


Display surface

Download
Links