eF-site ID 1cg2-ABCD
PDB Code 1cg2
Chain A, B, C, D

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Title CARBOXYPEPTIDASE G2
Classification METALLOCARBOXYPEPTIDASE
Compound CARBOXYPEPTIDASE G2
Source Pseudomonas sp. (strain RS-16) (CBPG_PSES6)
Sequence A:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA
AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK
NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG
NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL
IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW
TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER
AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK
EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH
SDKAEYVDISAIPRRLYMAARLIMDLGAG
B:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA
AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK
NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG
NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL
IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW
TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER
AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK
EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH
SDKAEYVDISAIPRRLYMAARLIMDLGAG
C:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA
AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK
NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG
NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL
IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW
TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER
AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK
EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH
SDKAEYVDISAIPRRLYMAARLIMDLGAG
D:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA
AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK
NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG
NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL
IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG
KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW
TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER
AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK
EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH
SDKAEYVDISAIPRRLYMAARLIMDLGAG
Description


Functional site

1) chain A
residue 112
type
sequence H
description CATALYTIC SITE.
source : CTA

2) chain A
residue 141
type
sequence D
description CATALYTIC SITE.
source : CTA

3) chain A
residue 176
type
sequence E
description CATALYTIC SITE.
source : CTA

4) chain A
residue 200
type
sequence E
description CATALYTIC SITE.
source : CTA

5) chain A
residue 385
type
sequence H
description CATALYTIC SITE.
source : CTA

6) chain B
residue 112
type
sequence H
description CATALYTIC SITE.
source : CTB

7) chain B
residue 141
type
sequence D
description CATALYTIC SITE.
source : CTB

8) chain B
residue 176
type
sequence E
description CATALYTIC SITE.
source : CTB

9) chain B
residue 200
type
sequence E
description CATALYTIC SITE.
source : CTB

10) chain B
residue 385
type
sequence H
description CATALYTIC SITE.
source : CTB

11) chain C
residue 112
type
sequence H
description CATALYTIC SITE.
source : CTC

12) chain C
residue 141
type
sequence D
description CATALYTIC SITE.
source : CTC

13) chain C
residue 176
type
sequence E
description CATALYTIC SITE.
source : CTC

14) chain C
residue 200
type
sequence E
description CATALYTIC SITE.
source : CTC

15) chain C
residue 385
type
sequence H
description CATALYTIC SITE.
source : CTC

16) chain D
residue 112
type
sequence H
description CATALYTIC SITE.
source : CTD

17) chain D
residue 141
type
sequence D
description CATALYTIC SITE.
source : CTD

18) chain D
residue 176
type
sequence E
description CATALYTIC SITE.
source : CTD

19) chain D
residue 200
type
sequence E
description CATALYTIC SITE.
source : CTD

20) chain D
residue 385
type
sequence H
description CATALYTIC SITE.
source : CTD

21) chain A
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 500
source : AC1

22) chain A
residue 176
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 500
source : AC1

23) chain A
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 500
source : AC1

24) chain A
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 501
source : AC2

25) chain A
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 501
source : AC2

26) chain A
residue 175
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 501
source : AC2

27) chain A
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 501
source : AC2

28) chain A
residue 229
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 502
source : AC3

29) chain C
residue 387
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 502
source : AC3

30) chain A
residue 256
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 503
source : AC4

31) chain B
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

32) chain B
residue 176
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

33) chain B
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 500
source : AC5

34) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

35) chain B
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

36) chain B
residue 175
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

37) chain B
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 501
source : AC6

38) chain B
residue 229
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 502
source : AC7

39) chain D
residue 387
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 502
source : AC7

40) chain C
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 500
source : AC8

41) chain C
residue 176
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 500
source : AC8

42) chain C
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 500
source : AC8

43) chain C
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 501
source : AC9

44) chain C
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 501
source : AC9

45) chain C
residue 175
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 501
source : AC9

46) chain C
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 501
source : AC9

47) chain A
residue 387
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 502
source : BC1

48) chain C
residue 229
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 502
source : BC1

49) chain D
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN D 500
source : BC2

50) chain D
residue 176
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 500
source : BC2

51) chain D
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 500
source : BC2

52) chain D
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 501
source : BC3

53) chain D
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE ZN D 501
source : BC3

54) chain D
residue 175
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 501
source : BC3

55) chain D
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 501
source : BC3

56) chain B
residue 387
type
sequence D
description BINDING SITE FOR RESIDUE ZN D 502
source : BC4

57) chain D
residue 229
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 502
source : BC4

58) chain A
residue 112
type catalytic
sequence H
description 447
source MCSA : MCSA1

59) chain A
residue 141
type catalytic
sequence D
description 447
source MCSA : MCSA1

60) chain A
residue 175
type catalytic
sequence E
description 447
source MCSA : MCSA1

61) chain A
residue 176
type catalytic
sequence E
description 447
source MCSA : MCSA1

62) chain A
residue 200
type catalytic
sequence E
description 447
source MCSA : MCSA1

63) chain A
residue 385
type catalytic
sequence H
description 447
source MCSA : MCSA1

64) chain B
residue 112
type catalytic
sequence H
description 447
source MCSA : MCSA2

65) chain B
residue 141
type catalytic
sequence D
description 447
source MCSA : MCSA2

66) chain B
residue 175
type catalytic
sequence E
description 447
source MCSA : MCSA2

67) chain B
residue 176
type catalytic
sequence E
description 447
source MCSA : MCSA2

68) chain B
residue 200
type catalytic
sequence E
description 447
source MCSA : MCSA2

69) chain B
residue 385
type catalytic
sequence H
description 447
source MCSA : MCSA2

70) chain C
residue 112
type catalytic
sequence H
description 447
source MCSA : MCSA3

71) chain C
residue 141
type catalytic
sequence D
description 447
source MCSA : MCSA3

72) chain C
residue 175
type catalytic
sequence E
description 447
source MCSA : MCSA3

73) chain C
residue 176
type catalytic
sequence E
description 447
source MCSA : MCSA3

74) chain C
residue 200
type catalytic
sequence E
description 447
source MCSA : MCSA3

75) chain C
residue 385
type catalytic
sequence H
description 447
source MCSA : MCSA3

76) chain D
residue 112
type catalytic
sequence H
description 447
source MCSA : MCSA4

77) chain D
residue 141
type catalytic
sequence D
description 447
source MCSA : MCSA4

78) chain D
residue 175
type catalytic
sequence E
description 447
source MCSA : MCSA4

79) chain D
residue 176
type catalytic
sequence E
description 447
source MCSA : MCSA4

80) chain D
residue 200
type catalytic
sequence E
description 447
source MCSA : MCSA4

81) chain D
residue 385
type catalytic
sequence H
description 447
source MCSA : MCSA4

82) chain A
residue 107-116
type prosite
sequence LLLMSHMDTV
description ARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. LLLMSHmDTV
source prosite : PS00758

83) chain A
residue 139-178
type prosite
sequence IADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKG
description ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. IADdKGgnAviLhtlkllkeygvrdygt.ItVLFntDEEkG
source prosite : PS00759

84) chain A
residue 114
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

85) chain B
residue 114
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

86) chain C
residue 114
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

87) chain D
residue 114
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

88) chain A
residue 175
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI2

89) chain B
residue 175
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI2

90) chain C
residue 175
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI2

91) chain D
residue 175
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI2

92) chain A
residue 112
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

93) chain B
residue 385
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

94) chain C
residue 112
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

95) chain C
residue 141
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

96) chain C
residue 176
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

97) chain C
residue 200
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

98) chain C
residue 385
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

99) chain D
residue 112
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

100) chain D
residue 141
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

101) chain D
residue 176
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

102) chain D
residue 200
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

103) chain A
residue 141
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

104) chain D
residue 385
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

105) chain A
residue 176
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

106) chain A
residue 200
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

107) chain A
residue 385
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

108) chain B
residue 112
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

109) chain B
residue 141
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

110) chain B
residue 176
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3

111) chain B
residue 200
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9083113
source Swiss-Prot : SWS_FT_FI3


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