eF-site ID 2yyt-ABCD
PDB Code 2yyt
Chain A, B, C, D

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Title Crystal structure of uncharacterized conserved protein from Geobacillus kaustophilus
Classification LYASE
Compound Orotidine 5'-phosphate decarboxylase
Source Geobacillus kaustophilus (PYRF_GEOKA)
Sequence A:  PFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQEGP
AIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGADL
VNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQLTS
TDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCSAN
EAAFIKERCGASFLAVTVTPRKARALGSDYIVIGRSLTRA
ADPLRTYARLQHEWN
B:  PFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQEGP
AIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGADL
VNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQLTS
TDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCSAN
EAAFIKERCGASFLAVTVTPRKARALGSDYIVIGRSLTRA
ADPLRTYARLQHEWN
C:  PFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQEGP
AIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGADL
VNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQLTS
TDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCSAN
EAAFIKERCGASFLAVTVTPRKARALGSDYIVIGRSLTRA
ADPLRTYARLQHEWN
D:  PFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQEGP
AIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGADL
VNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQLTS
TDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCSAN
EAAFIKERCGASFLAVTVTPRKARALGSDYIVIGRSLTRA
ADPLRTYARLQHEWN
Description


Functional site

1) chain A
residue 63
type ACT_SITE
sequence K
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 63
type ACT_SITE
sequence K
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 63
type ACT_SITE
sequence K
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 63
type ACT_SITE
sequence K
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 12
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 34
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

7) chain B
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

8) chain B
residue 124
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 215
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

10) chain B
residue 216
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

11) chain C
residue 12
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

12) chain C
residue 34
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

13) chain C
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 34
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

15) chain C
residue 124
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

16) chain C
residue 215
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

17) chain C
residue 216
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

18) chain D
residue 12
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

19) chain D
residue 34
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

20) chain D
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

21) chain D
residue 124
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 61
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

23) chain D
residue 215
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

24) chain D
residue 216
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 124
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 215
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 216
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 12
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01200
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 58-71
type prosite
sequence VFLDLKLHDIPNTV
description OMPDECASE Orotidine 5'-phosphate decarboxylase active site. VFlDlKlhDIPnTV
source prosite : PS00156


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