eF-site ID 6h8n-AB
PDB Code 6h8n
Chain A, B

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Title Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S
Classification HYDROLASE
Compound Peptidoglycan-N-acetylmuramic acid deacetylase PdaC
Source (PDAC_BACSU)
Sequence A:  VDPNQKVIALTFSDGPNPATTNQILDSLKKYKGHATFFVL
GSRVQYYPETLIRMLKEGNEVGNHSWSHPLLTRLSVKEAL
KQINDTQDIIEKISGYRPTLVRPPYGGINDELRSQMKMDV
ALWDVDPEDWKDRNKKTIVDRVMNQAGDGRTILIHDIYRT
SADAADEIIKKLTDQGYQLVTVSQLEEVKKQREAKELRRQ
WS
B:  VDPNQKVIALTFSDGPNPATTNQILDSLKKYKGHATFFVL
GSRVQYYPETLIRMLKEGNEVGNHSWSHPLLTRLSVKEAL
KQINDTQDIIEKISGYRPTLVRPPYGGINDELRSQMKMDV
ALWDVDPEDWKDRNKKTIVDRVMNQAGDGRTILIHDIYRT
SADAADEIIKKLTDQGYQLVTVSQLEEVKKQREAKELRRQ
WSHPQF
Description


Functional site

1) chain A
residue 261
type
sequence D
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 311
type
sequence H
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 315
type
sequence H
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 261
type
sequence D
description binding site for residue PO4 A 502
source : AC2

5) chain A
residue 311
type
sequence H
description binding site for residue PO4 A 502
source : AC2

6) chain A
residue 315
type
sequence H
description binding site for residue PO4 A 502
source : AC2

7) chain A
residue 351
type
sequence P
description binding site for residue PO4 A 502
source : AC2

8) chain A
residue 352
type
sequence Y
description binding site for residue PO4 A 502
source : AC2

9) chain A
residue 400
type
sequence L
description binding site for residue PO4 A 502
source : AC2

10) chain A
residue 402
type
sequence H
description binding site for residue PO4 A 502
source : AC2

11) chain B
residue 443
type
sequence E
description binding site for residue PO4 A 502
source : AC2

12) chain B
residue 446
type
sequence R
description binding site for residue PO4 A 502
source : AC2

13) chain A
residue 322
type
sequence S
description binding site for residue PO4 A 503
source : AC3

14) chain A
residue 324
type
sequence K
description binding site for residue PO4 A 503
source : AC3

15) chain A
residue 325
type
sequence E
description binding site for residue PO4 A 503
source : AC3

16) chain B
residue 379
type
sequence D
description binding site for residue PO4 A 503
source : AC3

17) chain B
residue 381
type
sequence N
description binding site for residue PO4 A 503
source : AC3

18) chain B
residue 384
type
sequence T
description binding site for residue PO4 A 503
source : AC3

19) chain A
residue 395
type
sequence D
description binding site for residue GOL A 504
source : AC4

20) chain A
residue 396
type
sequence G
description binding site for residue GOL A 504
source : AC4

21) chain A
residue 397
type
sequence R
description binding site for residue GOL A 504
source : AC4

22) chain B
residue 395
type
sequence D
description binding site for residue GOL A 504
source : AC4

23) chain B
residue 396
type
sequence G
description binding site for residue GOL A 504
source : AC4

24) chain B
residue 397
type
sequence R
description binding site for residue GOL A 504
source : AC4

25) chain B
residue 436
type
sequence K
description binding site for residue GOL A 504
source : AC4

26) chain A
residue 287
type
sequence L
description binding site for residue GOL B 501
source : AC5

27) chain A
residue 352
type
sequence Y
description binding site for residue GOL B 501
source : AC5

28) chain B
residue 446
type
sequence R
description binding site for residue GOL B 501
source : AC5

29) chain B
residue 261
type
sequence D
description binding site for residue ZN B 502
source : AC6

30) chain B
residue 311
type
sequence H
description binding site for residue ZN B 502
source : AC6

31) chain B
residue 315
type
sequence H
description binding site for residue ZN B 502
source : AC6

32) chain A
residue 443
type
sequence E
description binding site for residue PO4 B 503
source : AC7

33) chain A
residue 446
type
sequence R
description binding site for residue PO4 B 503
source : AC7

34) chain B
residue 261
type
sequence D
description binding site for residue PO4 B 503
source : AC7

35) chain B
residue 311
type
sequence H
description binding site for residue PO4 B 503
source : AC7

36) chain B
residue 315
type
sequence H
description binding site for residue PO4 B 503
source : AC7

37) chain B
residue 351
type
sequence P
description binding site for residue PO4 B 503
source : AC7

38) chain B
residue 352
type
sequence Y
description binding site for residue PO4 B 503
source : AC7

39) chain B
residue 400
type
sequence L
description binding site for residue PO4 B 503
source : AC7

40) chain B
residue 402
type
sequence H
description binding site for residue PO4 B 503
source : AC7

41) chain A
residue 260
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 260
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 402
type ACT_SITE
sequence H
description Proton donor => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 402
type ACT_SITE
sequence H
description Proton donor => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 261
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 311
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 315
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

48) chain B
residue 261
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 311
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 315
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

51) chain A
residue 376
type SITE
sequence D
description Raises pKa of active site His => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

52) chain B
residue 376
type SITE
sequence D
description Raises pKa of active site His => ECO:0000250
source Swiss-Prot : SWS_FT_FI4


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