eF-site ID 1umf-ABCD
PDB Code 1umf
Chain A, B, C, D

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Title crystal structure of chorismate synthase
Classification LYASE
Compound Chorismate synthase
Source Helicobacter pylori (Campylobacter pylori) (AROC_HELPY)
Sequence A:  MNTLGRFLRLTTFGESHGDVIGGVLDGMPSGIKIDYALLE
NEMKRRQGGRNVFITPRKEDDKVEITSGVFEDFSTGTPIG
FLIHNQRARSKDYDNIKNLFRPSHADFTYFHKYGIRDFRG
GGRSSARESAIRVAAGAFAKMLLREIGIVCESGIIEIGGI
KAKNYDFNHALKSEIFALDEEQEEAQKTAIQNAIKNHDSI
GGVALIRARSIKTNQKLPIGLGQGLYAKLDAKIAEAMMGL
NGVKAVEIGKGVESSLLKGSEYNDLMDQKGFLSNRSGGVL
GGMSNGEEIIVRVHFKPTPSIFQPQRTIDINGNECECLLK
GRHDPCIAIRGSVVCESLLALVLADMVLLNLTSKIEYLKT
IYNEN
B:  MNTLGRFLRLTTFGESHGDVIGGVLDGMPSGIKIDYALLE
NEMKRRQGGRNVFITPRKEDDKVEITSGVFEDFSTGTPIG
FLIHNQRARSKDYDNIKNLFRPSHADFTYFHKYGIRDFRG
GGRSSARESAIRVAAGAFAKMLLREIGIVCESGIIEIGGI
KAKNYDFNHALKSEIFALDEEQEEAQKTAIQNAIKNHDSI
GGVALIRARSIKTNQKLPIGLGQGLYAKLDAKIAEAMMGL
NGVKAVEIGKGVESSLLKGSEYNDLMDQKGFLSNRSGGVL
GGMSNGEEIIVRVHFKPTPSIFQPQRTIDINGNECECLLK
GRHDPCIAIRGSVVCESLLALVLADMVLLNLTSKIEYLKT
IYNEN
C:  MNTLGRFLRLTTFGESHGDVIGGVLDGMPSGIKIDYALLE
NEMKRRQGGRNVFITPRKEDDKVEITSGVFEDFSTGTPIG
FLIHNQRARSKDYDNIKNLFRPSHADFTYFHKYGIRDFRG
GGRSSARESAIRVAAGAFAKMLLREIGIVCESGIIEIGGI
KAKNYDFNHALKSEIFALDEEQEEAQKTAIQNAIKNHDSI
GGVALIRARSIKTNQKLPIGLGQGLYAKLDAKIAEAMMGL
NGVKAVEIGKGVESSLLKGSEYNDLMDQKGFLSNRSGGVL
GGMSNGEEIIVRVHFKPTPSIFQPQRTIDINGNECECLLK
GRHDPCIAIRGSVVCESLLALVLADMVLLNLTSKIEYLKT
IYNEN
D:  MNTLGRFLRLTTFGESHGDVIGGVLDGMPSGIKIDYALLE
NEMKRRQGGRNVFITPRKEDDKVEITSGVFEDFSTGTPIG
FLIHNQRARSKDYDNIKNLFRPSHADFTYFHKYGIRDFRG
GGRSSARESAIRVAAGAFAKMLLREIGIVCESGIIEIGGI
KAKNYDFNHALKSEIFALDEEQEEAQKTAIQNAIKNHDSI
GGVALIRARSIKTNQKLPIGLGQGLYAKLDAKIAEAMMGL
NGVKAVEIGKGVESSLLKGSEYNDLMDQKGFLSNRSGGVL
GGMSNGEEIIVRVHFKPTPSIFQPQRTIDINGNECECLLK
GRHDPCIAIRGSVVCESLLALVLADMVLLNLTSKIEYLKT
IYNEN
Description


Functional site

1) chain A
residue 14-29
type prosite
sequence GESHGDVIGGVLDGMP
description CHORISMATE_SYNTHASE_1 Chorismate synthase signature 1. GESHGdvIGgVLDGmP
source prosite : PS00787

2) chain A
residue 122-138
type prosite
sequence GRSSARESAIRVAAGAF
description CHORISMATE_SYNTHASE_2 Chorismate synthase signature 2. GrsSAReSairVaaGAF
source prosite : PS00788

3) chain A
residue 322-338
type prosite
sequence RHDPCIAIRGSVVCESL
description CHORISMATE_SYNTHASE_3 Chorismate synthase signature 3. RHDPCiairGsVVcESL
source prosite : PS00789

4) chain A
residue 46
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

5) chain C
residue 241
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

6) chain C
residue 281
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

7) chain C
residue 322
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

8) chain D
residue 46
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

9) chain D
residue 241
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

10) chain D
residue 281
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

11) chain D
residue 322
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 241
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 281
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 322
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 46
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 241
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

17) chain B
residue 281
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 322
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

19) chain C
residue 46
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 123
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 296
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

22) chain B
residue 123
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 296
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

24) chain C
residue 123
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

25) chain C
residue 296
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

26) chain D
residue 123
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2

27) chain D
residue 296
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:15095868
source Swiss-Prot : SWS_FT_FI2


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