eF-site ID 6nkj-AB
PDB Code 6nkj
Chain A, B

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Title 1.3 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Streptococcus pneumoniae in Complex with (2R)-2-(phosphonooxy)propanoic acid.
Classification TRANSFERASE
Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1
Source (MURA1_STRPN)
Sequence A:  MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGK
TVLQNVPILSDVFIMNQVVGGLNAKVDFDEEAHLVKVDAT
GDITEEAPYKYVSKMRASIVVLGPILARVGHAKVSMPGGC
TIGSRPIDLHLKGLEAMGVKISQTAGYIEAKAERLHGAHI
YMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI
LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAG
TFMVAAAMTGGDVLIRDAVWEHNRPLIAKLLEMGVEVIEE
DEGIRVRSQLENLKAVHVKTLPHPGFPTDMQAQFTALMTV
AKGESTMVETVFENRFQHLEEMRRMGLHSEIIRDTARIVG
GQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD
RGYYGFHEKLAQLGAKIQRIE
B:  MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGK
TVLQNVPILSDVFIMNQVVGGLNAKVDFDEEAHLVKVDAT
GDITEEAPYKYVSKMRASIVVLGPILARVGHAKVSMPGGC
TIGSRPIDLHLKGLEAMGVKISQTAGYIEAKAERLHGAHI
YMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI
LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAG
TFMVAAAMTGGDVLIRDAVWEHNRPLIAKLLEMGVEVIEE
DEGIRVRSQLENLKAVHVKTLPHPGFPTDMQAQFTALMTV
AKGESTMVETVFENRFQHLEEMRRMGLHSEIIRDTARIVG
GQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD
RGYYGFHEKLAQLGAKIQRIE
Description


Functional site

1) chain A
residue 96
type
sequence R
description binding site for residue 0V5 A 501
source : AC1

2) chain A
residue 120
type
sequence C
description binding site for residue 0V5 A 501
source : AC1

3) chain A
residue 121
type
sequence T
description binding site for residue 0V5 A 501
source : AC1

4) chain A
residue 401
type
sequence R
description binding site for residue 0V5 A 501
source : AC1

5) chain A
residue 23
type
sequence K
description binding site for residue CIT A 502
source : AC2

6) chain A
residue 24
type
sequence N
description binding site for residue CIT A 502
source : AC2

7) chain A
residue 122
type
sequence I
description binding site for residue CIT A 502
source : AC2

8) chain A
residue 125
type
sequence R
description binding site for residue CIT A 502
source : AC2

9) chain A
residue 309
type
sequence D
description binding site for residue CIT A 502
source : AC2

10) chain A
residue 335
type
sequence R
description binding site for residue CIT A 502
source : AC2

11) chain A
residue 374
type
sequence L
description binding site for residue CIT A 502
source : AC2

12) chain A
residue 375
type
sequence R
description binding site for residue CIT A 502
source : AC2

13) chain A
residue 401
type
sequence R
description binding site for residue CIT A 502
source : AC2

14) chain A
residue 115
type
sequence S
description binding site for residue CL A 503
source : AC3

15) chain A
residue 146
type
sequence G
description binding site for residue CL A 503
source : AC3

16) chain A
residue 147
type
sequence Y
description binding site for residue CL A 503
source : AC3

17) chain B
residue 344
type
sequence R
description binding site for residue CL A 503
source : AC3

18) chain B
residue 226
type
sequence H
description binding site for residue EDO B 502
source : AC4

19) chain B
residue 299
type
sequence K
description binding site for residue EDO B 502
source : AC4

20) chain B
residue 23
type
sequence K
description binding site for residue CIT B 503
source : AC5

21) chain B
residue 24
type
sequence N
description binding site for residue CIT B 503
source : AC5

22) chain B
residue 122
type
sequence I
description binding site for residue CIT B 503
source : AC5

23) chain B
residue 125
type
sequence R
description binding site for residue CIT B 503
source : AC5

24) chain B
residue 309
type
sequence D
description binding site for residue CIT B 503
source : AC5

25) chain B
residue 332
type
sequence F
description binding site for residue CIT B 503
source : AC5

26) chain B
residue 335
type
sequence R
description binding site for residue CIT B 503
source : AC5

27) chain B
residue 374
type
sequence L
description binding site for residue CIT B 503
source : AC5

28) chain B
residue 375
type
sequence R
description binding site for residue CIT B 503
source : AC5

29) chain B
residue 401
type
sequence R
description binding site for residue CIT B 503
source : AC5

30) chain B
residue 203
type
sequence N
description binding site for residue CL B 504
source : AC6

31) chain A
residue 340
type
sequence E
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

32) chain B
residue 96
type
sequence R
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

33) chain B
residue 119
type
sequence G
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

34) chain B
residue 121
type
sequence T
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

35) chain B
residue 122
type
sequence I
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

36) chain B
residue 123
type
sequence G
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

37) chain B
residue 125
type
sequence R
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

38) chain B
residue 401
type
sequence R
description binding site for Di-peptide 0V5 B 501 and CYS B 120
source : AC7

39) chain A
residue 120
type ACT_SITE
sequence C
description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI1

40) chain B
residue 120
type ACT_SITE
sequence C
description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 23
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 331
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 96
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 125
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 309
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 331
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 23
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 96
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 125
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 309
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 120
type MOD_RES
sequence C
description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI3

52) chain B
residue 120
type MOD_RES
sequence C
description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI3


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