eF-site ID 3wd4-A
PDB Code 3wd4
Chain A

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Title Serratia marcescens Chitinase B complexed with azide inhibitor and quinoline compound
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Chitinase B
Source Serratia marcescens (CHIB_SERMA)
Sequence A:  STRKAVIGYYFIPTNQINNYTETDTSVVPFPVSNITPAKA
KQLTHINFSFLDINSNLECAWDPATNDAKARDVVNRLTAL
KAHNPSLRIMFSIGGWYYSNDLGVSHANYVNAVKTPAART
KFAQSCVRIMKDYGFDGVDIDWEYPQAAEVDGFIAALQEI
RTLLNQQTIADGRQALPYQLTIAGAGGAFFLSRYYSKLAQ
IVAPLDYINLMTYDLAGPWEKITNHQAALFGDAAGPTFYN
ALREANLGWSWEELTRAFPSPFSLTVDAAVQQHLMMEGVP
SAKIVMGVPFYGRAFKGVSGGNGGQYSSHSTPGEDPYPNA
DYWLVGCDECVRDKDPRIASYRQLEQMLQGNYGYQRLWND
KTKTPYLYHAQNGLFVTYDDAESFKYKAKYIKQQQLGGVM
FWHLGQDNRNGDLLAALDRYFNAADYDDSQLDMGTGLRYT
GVGPGNLPIMTAPAYVPGTTYAQGALVSYQGYVWQTKWGY
ITSAPGSDSAWLKVGRL
Description


Functional site

1) chain A
residue 4
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 501
source : AC1

2) chain A
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 501
source : AC1

3) chain A
residue 89
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 501
source : AC1

4) chain A
residue 260
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

5) chain A
residue 263
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

6) chain A
residue 264
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

7) chain A
residue 439
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

8) chain A
residue 440
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

9) chain A
residue 441
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 502
source : AC2

10) chain A
residue 244
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 503
source : AC3

11) chain A
residue 252
type
sequence W
description BINDING SITE FOR RESIDUE GOL A 503
source : AC3

12) chain A
residue 259
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 503
source : AC3

13) chain A
residue 260
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 503
source : AC3

14) chain A
residue 261
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 503
source : AC3

15) chain A
residue 323
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

16) chain A
residue 325
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

17) chain A
residue 326
type
sequence V
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

18) chain A
residue 327
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

19) chain A
residue 328
type
sequence C
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

20) chain A
residue 329
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

21) chain A
residue 332
type
sequence V
description BINDING SITE FOR RESIDUE GOL A 504
source : AC4

22) chain A
residue 162
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 505
source : AC5

23) chain A
residue 204
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 505
source : AC5

24) chain A
residue 205
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 505
source : AC5

25) chain A
residue 207
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 505
source : AC5

26) chain A
residue 284
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 505
source : AC5

27) chain A
residue 393
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

28) chain A
residue 421
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

29) chain A
residue 427
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

30) chain A
residue 428
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

31) chain A
residue 429
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

32) chain A
residue 430
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 506
source : AC6

33) chain A
residue 359
type
sequence W
description BINDING SITE FOR RESIDUE GOL A 507
source : AC7

34) chain A
residue 360
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 507
source : AC7

35) chain A
residue 361
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 507
source : AC7

36) chain A
residue 362
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 507
source : AC7

37) chain A
residue 463
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 508
source : AC8

38) chain A
residue 464
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 508
source : AC8

39) chain A
residue 480
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 508
source : AC8

40) chain A
residue 481
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 508
source : AC8

41) chain A
residue 231
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

42) chain A
residue 391
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

43) chain A
residue 394
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

44) chain A
residue 395
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

45) chain A
residue 434
type
sequence M
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

46) chain A
residue 439
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 509
source : AC9

47) chain A
residue 386
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 510
source : BC1

48) chain A
residue 420
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 510
source : BC1

49) chain A
residue 427
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 510
source : BC1

50) chain A
residue 10
type
sequence Y
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

51) chain A
residue 12
type
sequence F
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

52) chain A
residue 97
type
sequence W
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

53) chain A
residue 142
type
sequence D
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

54) chain A
residue 144
type
sequence E
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

55) chain A
residue 212
type
sequence M
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

56) chain A
residue 214
type
sequence Y
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

57) chain A
residue 215
type
sequence D
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

58) chain A
residue 219
type
sequence P
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

59) chain A
residue 292
type
sequence Y
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

60) chain A
residue 294
type
sequence R
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

61) chain A
residue 338
type
sequence R
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

62) chain A
residue 403
type
sequence W
description BINDING SITE FOR RESIDUE A1L A 511
source : BC2

63) chain A
residue 97
type
sequence W
description BINDING SITE FOR RESIDUE QUB A 512
source : BC3

64) chain A
residue 191
type
sequence F
description BINDING SITE FOR RESIDUE QUB A 512
source : BC3

65) chain A
residue 219
type
sequence P
description BINDING SITE FOR RESIDUE QUB A 512
source : BC3

66) chain A
residue 220
type
sequence W
description BINDING SITE FOR RESIDUE QUB A 512
source : BC3

67) chain A
residue 316
type
sequence D
description BINDING SITE FOR RESIDUE QUB A 512
source : BC3

68) chain A
residue 68
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI2

69) chain A
residue 95
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI2

70) chain A
residue 145
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 212
type BINDING
sequence M
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI2

72) chain A
residue 403
type BINDING
sequence W
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI2

73) chain A
residue 144
type ACT_SITE
sequence E
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
source Swiss-Prot : SWS_FT_FI1

74) chain A
residue 136-144
type prosite
sequence FDGVDIDWE
description GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE
source prosite : PS01095


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