eF-site ID 1ci7-AB
PDB Code 1ci7
Chain A, B

click to enlarge
Title TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII
Classification TRANSFERASE
Compound PROTEIN (THYMIDYLATE SYNTHASE)
Source Pneumocystis carinii (TYSY_PNECA)
Sequence A:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF
SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK
NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA
EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP
ADLEKMALPPCHMFCQFYVHIPSRPELSCQLYQRSCDMGL
GVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIYKDH
IEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNIQNY
HPYETIKMKMSI
B:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF
SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK
NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA
EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP
ADLEKMALPPCHMFCQFYVHIPSRPELSCQLYQRSCDMGL
GVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIYKDH
IEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNIQNY
HPYETIKMKMSI
Description


Functional site

1) chain A
residue 153
type
sequence R
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

2) chain A
residue 154
type
sequence R
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

3) chain B
residue 26
type
sequence R
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

4) chain B
residue 170
type
sequence L
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

5) chain B
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

6) chain B
residue 199
type
sequence R
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

7) chain B
residue 200
type
sequence S
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

8) chain B
residue 201
type
sequence C
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

9) chain B
residue 202
type
sequence D
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

10) chain B
residue 210
type
sequence N
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

11) chain B
residue 240
type
sequence H
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

12) chain B
residue 242
type
sequence Y
description BINDING SITE FOR RESIDUE UMP B 765
source : AC1

13) chain A
residue 26
type
sequence R
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

14) chain A
residue 170
type
sequence L
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

15) chain A
residue 173
type
sequence C
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

16) chain A
residue 199
type
sequence R
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

17) chain A
residue 200
type
sequence S
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

18) chain A
residue 201
type
sequence C
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

19) chain A
residue 202
type
sequence D
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

20) chain A
residue 210
type
sequence N
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

21) chain A
residue 240
type
sequence H
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

22) chain A
residue 242
type
sequence Y
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

23) chain B
residue 153
type
sequence R
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

24) chain B
residue 154
type
sequence R
description BINDING SITE FOR RESIDUE UMP A 767
source : AC2

25) chain A
residue 56
type
sequence R
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

26) chain A
residue 58
type
sequence F
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

27) chain A
residue 86
type
sequence I
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

28) chain A
residue 90
type
sequence N
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

29) chain A
residue 202
type
sequence D
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

30) chain A
residue 206
type
sequence G
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

31) chain A
residue 209
type
sequence F
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

32) chain A
residue 210
type
sequence N
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

33) chain A
residue 242
type
sequence Y
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

34) chain A
residue 295
type
sequence M
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

35) chain A
residue 296
type
sequence S
description BINDING SITE FOR RESIDUE CB3 A 768
source : AC3

36) chain A
residue 173
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI1

37) chain B
residue 173
type ACT_SITE
sequence C
description Nucleophile => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 26
type BINDING
sequence R
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 199
type BINDING
sequence R
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 210
type BINDING
sequence N
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 240
type BINDING
sequence H
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 26
type BINDING
sequence R
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 199
type BINDING
sequence R
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 210
type BINDING
sequence N
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 240
type BINDING
sequence H
description in other chain => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 153
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 202
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI3

48) chain B
residue 153
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 202
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P0A884
source Swiss-Prot : SWS_FT_FI3

50) chain A
residue 153-181
type prosite
sequence RRLILSAWNPADLEKMALPPCHMFCQFYV
description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIlsaWNpadlekma.....LpPCHmfcQFyV
source prosite : PS00091


Display surface

Download
Links