eF-site ID 2glv-ABCDEFGHIJKL
PDB Code 2glv
Chain A, B, C, D, E, F, G, H, I, J, K, L

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Title Crystal structure of (3R)-Hydroxyacyl-Acyl Carrier Protein Dehydratase(FabZ) mutant(Y100A) from Helicobacter pylori
Classification LYASE
Compound (3R)-hydroxymyristoyl-acyl carrier protein dehydratase
Source Helicobacter pylori (Campylobacter pylori) (Q5G940_HELPY)
Sequence A:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
B:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAE
C:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
D:  QSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNI
TFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWG
FDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLKH
KGMIWQVGGTAQVDGKVVAEAELKAMIAERE
E:  QSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNI
TFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWG
FDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLKH
KGMIWQVGGTAQVDGKVVAEAELKAMIAERE
F:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
G:  QSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNI
TFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWG
FDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLKH
KGMIWQVGGTAQVDGKVVAEAELKAMIAER
H:  SQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNIT
FNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGF
DPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLKHK
GMIWQVGGTAQVDGKVVAEAELKAMIAE
I:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
J:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
K:  LQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKN
ITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLW
GFDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLK
HKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
L:  QSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNI
TFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWG
FDPEIAKTKIVAFMTIDKVKFRIPVTPGDRLEYHLEVLKH
KGMIWQVGGTAQVDGKVVAEAELKAMIAERE
Description


Functional site

1) chain A
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL B 1001
source : AC1

2) chain B
residue 58
type
sequence H
description BINDING SITE FOR RESIDUE CL B 1001
source : AC1

3) chain B
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL B 1001
source : AC1

4) chain I
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL I 1002
source : AC2

5) chain E
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL E 1003
source : AC3

6) chain F
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL E 1003
source : AC3

7) chain E
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL F 1004
source : AC4

8) chain F
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL F 1004
source : AC4

9) chain K
residue 58
type
sequence H
description BINDING SITE FOR RESIDUE CL K 1005
source : AC5

10) chain K
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL K 1005
source : AC5

11) chain L
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL K 1005
source : AC5

12) chain K
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL K 1006
source : AC6

13) chain L
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL K 1006
source : AC6

14) chain I
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL I 1007
source : AC7

15) chain G
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL G 1008
source : AC8

16) chain H
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1008
source : AC8

17) chain G
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL G 1009
source : AC9

18) chain A
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL A 1010
source : BC1

19) chain C
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL C 1011
source : BC2

20) chain D
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL C 1011
source : BC2

21) chain C
residue 101
type
sequence F
description BINDING SITE FOR RESIDUE CL D 1012
source : BC3

22) chain D
residue 58
type
sequence H
description BINDING SITE FOR RESIDUE CL D 1012
source : BC3

23) chain D
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE CL D 1012
source : BC3

24) chain A
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

25) chain J
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

26) chain K
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

27) chain L
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

29) chain C
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

30) chain D
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

31) chain E
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

32) chain F
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

33) chain G
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

34) chain H
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1

35) chain I
residue 58
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00406
source Swiss-Prot : SWS_FT_FI1


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