eF-site ID 3cmc-P
PDB Code 3cmc
Chain P

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Title Thioacylenzyme intermediate of Bacillus stearothermophilus phosphorylating GAPDH
Classification OXIDOREDUCTASE
Compound Glyceraldehyde-3-phosphate dehydrogenase
Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (G3P_BACST)
Sequence P:  AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTL
AHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPE
NLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISA
PAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFA
KVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAA
AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSV
VDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLV
SRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSH
RVVDLAAYIASKGL
Description (1)  Glyceraldehyde-3-phosphate dehydrogenase (E.C.1.2.1.12)


Functional site

1) chain P
residue 121
type
sequence P
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

2) chain P
residue 148
type
sequence S
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

3) chain P
residue 207
type
sequence T
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

4) chain P
residue 208
type
sequence T
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

5) chain P
residue 209
type
sequence G
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

6) chain P
residue 210
type
sequence A
description BINDING SITE FOR RESIDUE SO4 P 401
source : AC2

7) chain P
residue 179
type
sequence T
description BINDING SITE FOR RESIDUE SO4 P 402
source : AC6

8) chain P
residue 181
type
sequence D
description BINDING SITE FOR RESIDUE SO4 P 402
source : AC6

9) chain P
residue 195
type
sequence R
description BINDING SITE FOR RESIDUE SO4 P 402
source : AC6

10) chain P
residue 231
type
sequence R
description BINDING SITE FOR RESIDUE SO4 P 402
source : AC6

11) chain P
residue 303
type
sequence K
description BINDING SITE FOR RESIDUE SO4 O 403
source : AC9

12) chain P
residue 138
type
sequence D
description BINDING SITE FOR RESIDUE SO4 R 407
source : BC8

13) chain P
residue 139
type
sequence K
description BINDING SITE FOR RESIDUE SO4 R 407
source : BC8

14) chain P
residue 148
type
sequence S
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

15) chain P
residue 149
type
sequence C
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

16) chain P
residue 150
type
sequence T
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

17) chain P
residue 176
type
sequence H
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

18) chain P
residue 208
type
sequence T
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

19) chain P
residue 209
type
sequence G
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

20) chain P
residue 231
type
sequence R
description BINDING SITE FOR RESIDUE G3H P 400
source : CC2

21) chain P
residue 7
type
sequence G
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

22) chain P
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

23) chain P
residue 10
type
sequence R
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

24) chain P
residue 11
type
sequence I
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

25) chain P
residue 31
type
sequence N
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

26) chain P
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

27) chain P
residue 33
type
sequence L
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

28) chain P
residue 77
type
sequence R
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

29) chain P
residue 95
type
sequence S
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

30) chain P
residue 96
type
sequence T
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

31) chain P
residue 97
type
sequence G
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

32) chain P
residue 119
type
sequence S
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

33) chain P
residue 120
type
sequence A
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

34) chain P
residue 180
type
sequence N
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

35) chain P
residue 313
type
sequence N
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

36) chain P
residue 317
type
sequence Y
description BINDING SITE FOR RESIDUE NAD P 403
source : CC6

37) chain P
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE GOL P 404
source : DC2

38) chain P
residue 134
type
sequence Q
description BINDING SITE FOR RESIDUE GOL P 404
source : DC2

39) chain P
residue 135
type
sequence D
description BINDING SITE FOR RESIDUE GOL P 404
source : DC2

40) chain P
residue 159
type
sequence K
description BINDING SITE FOR RESIDUE GOL P 404
source : DC2

41) chain P
residue 181
type
sequence D
description BINDING SITE FOR RESIDUE GOL P 405
source : DC3

42) chain P
residue 183
type
sequence R
description BINDING SITE FOR RESIDUE GOL P 405
source : DC3

43) chain P
residue 188
type
sequence P
description BINDING SITE FOR RESIDUE GOL P 405
source : DC3

44) chain P
residue 190
type
sequence H
description BINDING SITE FOR RESIDUE GOL P 405
source : DC3

45) chain P
residue 191
type
sequence K
description BINDING SITE FOR RESIDUE GOL P 405
source : DC3

46) chain P
residue 169
type
sequence R
description BINDING SITE FOR RESIDUE GOL O 408
source : DC4

47) chain P
residue 212
type
sequence K
description BINDING SITE FOR RESIDUE GOL P 406
source : DC6

48) chain P
residue 215
type
sequence A
description BINDING SITE FOR RESIDUE GOL P 406
source : DC6

49) chain P
residue 223
type
sequence G
description BINDING SITE FOR RESIDUE GOL P 406
source : DC6

50) chain P
residue 50
type
sequence H
description BINDING SITE FOR RESIDUE GOL P 407
source : DC8

51) chain P
residue 51
type
sequence G
description BINDING SITE FOR RESIDUE GOL P 407
source : DC8

52) chain P
residue 208
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI5

53) chain P
residue 149
type ACT_SITE
sequence C
description Nucleophile => ECO:0000269|PubMed:18480053, ECO:0000305|PubMed:12569100
source Swiss-Prot : SWS_FT_FI1

54) chain P
residue 119
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

55) chain P
residue 180
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

56) chain P
residue 313
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

57) chain P
residue 10
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

58) chain P
residue 32
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

59) chain P
residue 77
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI2

60) chain P
residue 148
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI3

61) chain P
residue 179
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI3

62) chain P
residue 231
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI3

63) chain P
residue 195
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:9175858
source Swiss-Prot : SWS_FT_FI4

64) chain P
residue 176
type SITE
sequence H
description Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8
source Swiss-Prot : SWS_FT_FI6


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