eF-site ID 1bs6-ABCDEF
PDB Code 1bs6
Chain A, B, C, D, E, F

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Title PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER
Classification HYDROLASE
Compound PROTEIN (PEPTIDE DEFORMYLASE)
Source Escherichia coli (strain K12) (1BS6)
Sequence A:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA
EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK
SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL
EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK
LDRLKARA
B:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA
EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK
SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL
EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK
LDRLKARA
C:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA
EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK
SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL
EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK
LDRLKARA
D:  MAS
E:  MAS
F:  MAS
Description


Functional site

1) chain A
residue 90
type
sequence C
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A
source : NIA

2) chain A
residue 132
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A
source : NIA

3) chain A
residue 136
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A
source : NIA

4) chain B
residue 590
type
sequence C
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B
source : NIB

5) chain B
residue 632
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B
source : NIB

6) chain B
residue 636
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B
source : NIB

7) chain C
residue 1090
type
sequence C
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C
source : NIC

8) chain C
residue 1132
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C
source : NIC

9) chain C
residue 1136
type
sequence H
description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C
source : NIC

10) chain B
residue 554
type
sequence H
description BINDING SITE FOR RESIDUE SO4 B 3001
source : AC1

11) chain B
residue 555
type
sequence Q
description BINDING SITE FOR RESIDUE SO4 B 3001
source : AC1

12) chain C
residue 1029
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 3001
source : AC1

13) chain B
residue 529
type
sequence R
description BINDING SITE FOR RESIDUE SO4 C 3002
source : AC2

14) chain C
residue 1053
type
sequence I
description BINDING SITE FOR RESIDUE SO4 C 3002
source : AC2

15) chain C
residue 1054
type
sequence H
description BINDING SITE FOR RESIDUE SO4 C 3002
source : AC2

16) chain C
residue 1055
type
sequence Q
description BINDING SITE FOR RESIDUE SO4 C 3002
source : AC2

17) chain A
residue 90
type
sequence C
description BINDING SITE FOR RESIDUE NI A 2001
source : AC3

18) chain A
residue 132
type
sequence H
description BINDING SITE FOR RESIDUE NI A 2001
source : AC3

19) chain A
residue 136
type
sequence H
description BINDING SITE FOR RESIDUE NI A 2001
source : AC3

20) chain B
residue 550
type
sequence Q
description BINDING SITE FOR RESIDUE NI B 2001
source : AC4

21) chain B
residue 590
type
sequence C
description BINDING SITE FOR RESIDUE NI B 2001
source : AC4

22) chain B
residue 632
type
sequence H
description BINDING SITE FOR RESIDUE NI B 2001
source : AC4

23) chain B
residue 636
type
sequence H
description BINDING SITE FOR RESIDUE NI B 2001
source : AC4

24) chain E
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE NI B 2001
source : AC4

25) chain C
residue 1050
type
sequence Q
description BINDING SITE FOR RESIDUE NI C 2001
source : AC5

26) chain C
residue 1090
type
sequence C
description BINDING SITE FOR RESIDUE NI C 2001
source : AC5

27) chain C
residue 1132
type
sequence H
description BINDING SITE FOR RESIDUE NI C 2001
source : AC5

28) chain C
residue 1136
type
sequence H
description BINDING SITE FOR RESIDUE NI C 2001
source : AC5

29) chain A
residue 46
type catalytic
sequence L
description 98
source MCSA : MCSA1

30) chain A
residue 51
type catalytic
sequence V
description 98
source MCSA : MCSA1

31) chain A
residue 91
type catalytic
sequence L
description 98
source MCSA : MCSA1

32) chain A
residue 92
type catalytic
sequence S
description 98
source MCSA : MCSA1

33) chain A
residue 133
type catalytic
sequence E
description 98
source MCSA : MCSA1

34) chain A
residue 134
type catalytic
sequence M
description 98
source MCSA : MCSA1

35) chain A
residue 137
type catalytic
sequence L
description 98
source MCSA : MCSA1

36) chain B
residue 546
type catalytic
sequence L
description 98
source MCSA : MCSA2

37) chain B
residue 551
type catalytic
sequence V
description 98
source MCSA : MCSA2

38) chain B
residue 591
type catalytic
sequence L
description 98
source MCSA : MCSA2

39) chain B
residue 592
type catalytic
sequence S
description 98
source MCSA : MCSA2

40) chain B
residue 633
type catalytic
sequence E
description 98
source MCSA : MCSA2

41) chain B
residue 634
type catalytic
sequence M
description 98
source MCSA : MCSA2

42) chain B
residue 637
type catalytic
sequence L
description 98
source MCSA : MCSA2

43) chain C
residue 1046
type catalytic
sequence L
description 98
source MCSA : MCSA3

44) chain C
residue 1051
type catalytic
sequence V
description 98
source MCSA : MCSA3

45) chain C
residue 1091
type catalytic
sequence L
description 98
source MCSA : MCSA3

46) chain C
residue 1092
type catalytic
sequence S
description 98
source MCSA : MCSA3

47) chain C
residue 1133
type catalytic
sequence E
description 98
source MCSA : MCSA3

48) chain C
residue 1134
type catalytic
sequence M
description 98
source MCSA : MCSA3

49) chain C
residue 1137
type catalytic
sequence L
description 98
source MCSA : MCSA3

50) chain A
residue 134
type ACT_SITE
sequence M
description ACT_SITE => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI1

51) chain B
residue 634
type ACT_SITE
sequence M
description ACT_SITE => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI1

52) chain C
residue 1134
type ACT_SITE
sequence M
description ACT_SITE => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 91
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 133
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 137
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

56) chain B
residue 591
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

57) chain B
residue 633
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

58) chain B
residue 637
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

59) chain C
residue 1091
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

60) chain C
residue 1133
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2

61) chain C
residue 1137
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9846875
source Swiss-Prot : SWS_FT_FI2


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