eF-site ID 117e-B
PDB Code 117e
Chain B

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Title THE R78K AND D117E ACTIVE SITE VARIANTS OF SACCHAROMYCES CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASE: STRUCTURAL STUDIES AND MECHANISTIC IMPLICATIONS
Classification HYDROLASE
Compound PROTEIN (INORGANIC PYROPHOSPHATASE)
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IPYR_YEAST)
Sequence B:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN
NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV
RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNEPID
VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI
NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE
NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI
DLTNVTLPDTPTYSKAASDAIPPASLKADAPIDKSIDKWF
FI
Description


Functional site

1) chain B
residue 1117
type
sequence E
description
source : MN5

2) chain B
residue 1152
type
sequence D
description
source : MN5

3) chain B
residue 1115
type
sequence D
description
source : MN5

4) chain B
residue 1120
type
sequence D
description
source : MN5

5) chain B
residue 1117
type
sequence E
description
source : MN6

6) chain B
residue 1093
type
sequence Y
description
source : MN6

7) chain B
residue 1120
type
sequence D
description
source : MN6

8) chain B
residue 1152
type
sequence D
description
source : MN8

9) chain B
residue 1147
type
sequence D
description
source : MN8

10) chain B
residue 1115
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2005
source : AC5

11) chain B
residue 1117
type
sequence E
description BINDING SITE FOR RESIDUE MN B 2005
source : AC5

12) chain B
residue 1120
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2005
source : AC5

13) chain B
residue 1152
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2005
source : AC5

14) chain B
residue 1117
type
sequence E
description BINDING SITE FOR RESIDUE MN B 2006
source : AC6

15) chain B
residue 1120
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2006
source : AC6

16) chain B
residue 1058
type
sequence E
description BINDING SITE FOR RESIDUE MN B 2007
source : AC7

17) chain B
residue 1117
type
sequence E
description BINDING SITE FOR RESIDUE MN B 2007
source : AC7

18) chain B
residue 1147
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2008
source : AC8

19) chain B
residue 1152
type
sequence D
description BINDING SITE FOR RESIDUE MN B 2008
source : AC8

20) chain B
residue 1056
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

21) chain B
residue 1093
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

22) chain B
residue 1115
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

23) chain B
residue 1117
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

24) chain B
residue 1120
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

25) chain B
residue 1152
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

26) chain B
residue 1154
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3004
source : BC2

27) chain B
residue 1090
type ACT_SITE
sequence I
description Proton donor => ECO:0000269|PubMed:1322842
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 1079
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 1116
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 1121
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 1153
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 1065
type MOD_RES
sequence L
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 1251
type MOD_RES
sequence P
description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
source Swiss-Prot : SWS_FT_FI4

34) chain B
residue 1266
type MOD_RES
sequence L
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI5

35) chain B
residue 1239
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI7

36) chain B
residue 1279
type CROSSLNK
sequence W
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI7


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