eF-site ID 6fpg-BCDEFGHI
PDB Code 6fpg
Chain B, C, D, E, F, G, H, I

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Title Structure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellin
Classification CELL INVASION
Compound Chromosome 16, whole genome shotgun sequence
Source (A0A1D6GNR3_MAIZE)
Sequence B:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG
RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR
PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT
NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL
LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT
DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL
FQAYLIPITTQIEAAAILDHANKC
C:  SEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRA
PSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPL
PPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNM
DEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLG
YPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDH
KQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQ
AYLIPITTQIEAAAILDHANKC
D:  TCQPSGSIQGRSGNCNECCKNGRRYTTYGCSPPVTGSTRA
VLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNGGS
RCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEPPC
RNNIVDGSPAVWDALGLNKDDGQAQITWSDELE
E:  TCQPSGSIQGRSGNCNTSECCKNGRRYTTYGCSPPVTGST
RAVLTLNSFAEGGDGGGAAACTGKFYDDSKKVVALSTGWY
NGGSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNF
EPPCRNNIVDGSPAVWDALGLNKDDGQAQITWSDELE
F:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG
RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR
PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT
NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL
LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT
DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL
FQAYLIPITTQIEAAAILDHANKCTL
G:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG
RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR
PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT
NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL
LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT
DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL
FQAYLIPITTQIEAAAILDHANKCT
H:  TCQPSGSIQGRSGNCNTEECCKNGRRYTTYGCSPPVTGST
RAVLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNG
GSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEP
PCRNNIVDGSPAVWDALGLNKDDGQAQITWSDEL
I:  TCQPSGSIQGRSGNCNTSECCKNGRRYTTYGCSPPVTGST
RAVLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNG
GSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEP
PCRNNIVDGSPAVWDALGLNKDDGQAQITWSDEL
Description


Functional site

1) chain C
residue 43
type
sequence R
description binding site for residue CIT C 301
source : AC1

2) chain C
residue 190
type
sequence I
description binding site for residue CIT C 301
source : AC1

3) chain C
residue 194
type
sequence K
description binding site for residue CIT C 301
source : AC1

4) chain C
residue 229
type
sequence Q
description binding site for residue CIT C 301
source : AC1

5) chain C
residue 278
type
sequence E
description binding site for residue CIT C 301
source : AC1

6) chain E
residue 160
type
sequence D
description binding site for residue CIT C 301
source : AC1

7) chain B
residue 43
type
sequence R
description binding site for residue CIT B 301
source : AC2

8) chain B
residue 194
type
sequence K
description binding site for residue CIT B 301
source : AC2

9) chain B
residue 229
type
sequence Q
description binding site for residue CIT B 301
source : AC2

10) chain B
residue 278
type
sequence E
description binding site for residue CIT B 301
source : AC2

11) chain D
residue 160
type
sequence D
description binding site for residue CIT B 301
source : AC2

12) chain F
residue 43
type
sequence R
description binding site for residue CIT F 301
source : AC3

13) chain F
residue 190
type
sequence I
description binding site for residue CIT F 301
source : AC3

14) chain F
residue 194
type
sequence K
description binding site for residue CIT F 301
source : AC3

15) chain F
residue 229
type
sequence Q
description binding site for residue CIT F 301
source : AC3

16) chain F
residue 278
type
sequence E
description binding site for residue CIT F 301
source : AC3

17) chain I
residue 160
type
sequence D
description binding site for residue CIT F 301
source : AC3

18) chain G
residue 43
type
sequence R
description binding site for residue CIT G 301
source : AC4

19) chain G
residue 190
type
sequence I
description binding site for residue CIT G 301
source : AC4

20) chain G
residue 194
type
sequence K
description binding site for residue CIT G 301
source : AC4

21) chain G
residue 229
type
sequence Q
description binding site for residue CIT G 301
source : AC4

22) chain G
residue 278
type
sequence E
description binding site for residue CIT G 301
source : AC4

23) chain H
residue 160
type
sequence D
description binding site for residue CIT G 301
source : AC4

24) chain C
residue 159
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

25) chain C
residue 208
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 159
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 208
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

28) chain F
residue 159
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

29) chain F
residue 208
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

30) chain G
residue 159
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1

31) chain G
residue 208
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI1


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