eF-site ID 1ga6-AI
PDB Code 1ga6
Chain A, I

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Title CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound SERINE-CARBOXYL PROTEINASE
Source Pseudomonas sp. (strain 101) (Achromobacter parvulus T1) (1GA6)
Sequence A:  AGTAKGHNPTEFPTIYDASSAPTAANTTVGIITIGGVSQT
LQDLQQFTSANGLASVNTQTIQTGSSNGDYSDDQQGQGEW
DLDSQSIVGSAGGAVQQLLFYMADQSASGNTGLTQAFNQA
VSDNVAKVINVSLGWCEADANADGTLQAEDRIFATAAAQG
QTFSVSSGDEGVYECNNRGYPDGSTYSVSWPASSPNVIAV
GGTTLYTTSAGAYSNETVWNEGLDSNGKLWATGGGYSVYE
SKPSWQSVVSGTPGRRLLPDISFDAAQGTGALIYNYGQLQ
QIGGTSLASPIFVGLWARLQSANSNSLGFPAASFYSAISS
TPSLVHDVKSGNNGYGGYGYNAGTGWDYPTGWGSLDIAKL
SAYIRSNGF
I:  YX
Description


Functional site

1) chain A
residue 328
type
sequence D
description BINDING SITE FOR RESIDUE CA A 374
source : AC1

2) chain A
residue 329
type
sequence V
description BINDING SITE FOR RESIDUE CA A 374
source : AC1

3) chain A
residue 344
type
sequence G
description BINDING SITE FOR RESIDUE CA A 374
source : AC1

4) chain A
residue 346
type
sequence G
description BINDING SITE FOR RESIDUE CA A 374
source : AC1

5) chain A
residue 348
type
sequence D
description BINDING SITE FOR RESIDUE CA A 374
source : AC1

6) chain A
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

7) chain A
residue 135
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

8) chain A
residue 167
type
sequence S
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

9) chain A
residue 169
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

10) chain A
residue 171
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

11) chain A
residue 179
type
sequence R
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

12) chain A
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE ACT A 395
source : AC2

13) chain A
residue 24
type
sequence T
description BINDING SITE FOR RESIDUE ACT A 396
source : AC3

14) chain A
residue 196
type
sequence P
description BINDING SITE FOR RESIDUE ACT A 396
source : AC3

15) chain A
residue 244
type
sequence P
description BINDING SITE FOR RESIDUE ACT A 396
source : AC3

16) chain A
residue 128
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 397
source : AC4

17) chain A
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 397
source : AC4

18) chain A
residue 307
type
sequence S
description BINDING SITE FOR RESIDUE ACT A 397
source : AC4

19) chain A
residue 308
type
sequence L
description BINDING SITE FOR RESIDUE ACT A 397
source : AC4

20) chain A
residue 309
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 397
source : AC4

21) chain A
residue 324
type
sequence S
description BINDING SITE FOR RESIDUE ACT A 398
source : AC5

22) chain A
residue 326
type
sequence V
description BINDING SITE FOR RESIDUE ACT A 398
source : AC5

23) chain A
residue 327
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 398
source : AC5

24) chain A
residue 357
type
sequence D
description BINDING SITE FOR RESIDUE ACT A 398
source : AC5

25) chain A
residue 360
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 398
source : AC5

26) chain A
residue 9
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

27) chain A
residue 48
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

28) chain A
residue 52
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

29) chain A
residue 186
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

30) chain A
residue 273
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

31) chain A
residue 275
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

32) chain A
residue 280
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 391
source : AC6

33) chain A
residue 20
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 392
source : AC7

34) chain A
residue 309
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 392
source : AC7

35) chain A
residue 314
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 392
source : AC7

36) chain A
residue 370
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 392
source : AC7

37) chain A
residue 125
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 393
source : AC8

38) chain A
residue 126
type
sequence V
description BINDING SITE FOR RESIDUE GOL A 393
source : AC8

39) chain A
residue 306
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 393
source : AC8

40) chain A
residue 5
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 394
source : AC9

41) chain A
residue 221
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 394
source : AC9

42) chain A
residue 222
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 394
source : AC9

43) chain A
residue 80
type catalytic
sequence E
description 380
source MCSA : MCSA1

44) chain A
residue 84
type catalytic
sequence D
description 380
source MCSA : MCSA1

45) chain A
residue 170
type catalytic
sequence D
description 380
source MCSA : MCSA1

46) chain A
residue 287
type catalytic
sequence S
description 380
source MCSA : MCSA1

47) chain A
residue 328
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 329
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 344
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 346
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 348
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 80
type ACT_SITE
sequence E
description Charge relay system => ECO:0000269|PubMed:10488127
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 84
type ACT_SITE
sequence D
description Charge relay system => ECO:0000269|PubMed:10488127
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 287
type ACT_SITE
sequence S
description Charge relay system => ECO:0000269|PubMed:10488127
source Swiss-Prot : SWS_FT_FI1

55) chain A
residue 285-295
type prosite
sequence GTSLASPIFVG
description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAsPiFVG
source prosite : PS00138


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