eF-site ID 2p2d-ABCD
PDB Code 2p2d
Chain A, B, C, D

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Title Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I
Classification TRANSFERASE
Compound L-ASPARAGINASE I
Source Escherichia coli (strain K12) (ASPG1_ECOLI)
Sequence A:  QKKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEF
HRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDD
YDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPL
AELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRT
TKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE
LIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRS
YGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMN
ALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAMS
QNLRGELTPD
B:  KKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEFH
RPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDDY
DGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLA
ELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTT
KAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGEL
IVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSY
GVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMNA
LAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAMSQ
NLRGELTPD
C:  QKKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEF
HRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDD
YDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPL
AELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRT
TKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE
LIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRS
YGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMG
NALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAM
SQNLRGELTPD
D:  MQKKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPE
FHRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYD
DYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIP
LAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNR
TTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEG
ELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILR
SYGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNM
NALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAM
SQNLRGELTPD
Description


Functional site

1) chain A
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

2) chain A
residue 105
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

3) chain A
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

4) chain A
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

5) chain A
residue 196
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

6) chain A
residue 331
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 7001
source : AC1

7) chain C
residue 176
type
sequence N
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

8) chain C
residue 271
type
sequence T
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

9) chain C
residue 274
type
sequence M
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

10) chain C
residue 275
type
sequence S
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

11) chain C
residue 276
type
sequence G
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

12) chain C
residue 300
type
sequence M
description BINDING SITE FOR RESIDUE GOL C 7002
source : AC2

13) chain C
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE GOL C 7003
source : AC3

14) chain C
residue 105
type
sequence L
description BINDING SITE FOR RESIDUE GOL C 7003
source : AC3

15) chain C
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE GOL C 7003
source : AC3

16) chain C
residue 196
type
sequence P
description BINDING SITE FOR RESIDUE GOL C 7003
source : AC3

17) chain C
residue 331
type
sequence R
description BINDING SITE FOR RESIDUE GOL C 7003
source : AC3

18) chain A
residue 240
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 7004
source : AC4

19) chain A
residue 271
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 7004
source : AC4

20) chain A
residue 273
type
sequence C
description BINDING SITE FOR RESIDUE GOL A 7004
source : AC4

21) chain A
residue 300
type
sequence M
description BINDING SITE FOR RESIDUE GOL A 7004
source : AC4

22) chain A
residue 302
type
sequence V
description BINDING SITE FOR RESIDUE GOL A 7004
source : AC4

23) chain D
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

24) chain D
residue 105
type
sequence L
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

25) chain D
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

26) chain D
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

27) chain D
residue 196
type
sequence P
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

28) chain D
residue 331
type
sequence R
description BINDING SITE FOR RESIDUE GOL D 7005
source : AC5

29) chain D
residue 176
type
sequence N
description BINDING SITE FOR RESIDUE GOL D 7006
source : AC6

30) chain D
residue 274
type
sequence M
description BINDING SITE FOR RESIDUE GOL D 7006
source : AC6

31) chain D
residue 275
type
sequence S
description BINDING SITE FOR RESIDUE GOL D 7006
source : AC6

32) chain D
residue 276
type
sequence G
description BINDING SITE FOR RESIDUE GOL D 7006
source : AC6

33) chain D
residue 300
type
sequence M
description BINDING SITE FOR RESIDUE GOL D 7006
source : AC6

34) chain B
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 7007
source : AC7

35) chain B
residue 105
type
sequence L
description BINDING SITE FOR RESIDUE GOL B 7007
source : AC7

36) chain B
residue 108
type
sequence L
description BINDING SITE FOR RESIDUE GOL B 7007
source : AC7

37) chain B
residue 196
type
sequence P
description BINDING SITE FOR RESIDUE GOL B 7007
source : AC7

38) chain B
residue 331
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 7007
source : AC7

39) chain B
residue 176
type
sequence N
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

40) chain B
residue 271
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

41) chain B
residue 274
type
sequence M
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

42) chain B
residue 275
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

43) chain B
residue 276
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

44) chain B
residue 300
type
sequence M
description BINDING SITE FOR RESIDUE GOL B 7008
source : AC8

45) chain A
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

46) chain A
residue 58
type
sequence M
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

47) chain A
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

48) chain A
residue 90
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

49) chain A
residue 91
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

50) chain A
residue 92
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 9001
source : AC9

51) chain B
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

52) chain B
residue 14
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

53) chain B
residue 59
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

54) chain B
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

55) chain B
residue 90
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

56) chain B
residue 91
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

57) chain B
residue 92
type
sequence D
description BINDING SITE FOR RESIDUE GOL B 9002
source : BC1

58) chain C
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

59) chain C
residue 14
type
sequence T
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

60) chain C
residue 58
type
sequence M
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

61) chain C
residue 59
type
sequence D
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

62) chain C
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

63) chain C
residue 90
type
sequence G
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

64) chain C
residue 91
type
sequence T
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

65) chain C
residue 92
type
sequence D
description BINDING SITE FOR RESIDUE GOL C 9003
source : BC2

66) chain D
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

67) chain D
residue 58
type
sequence M
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

68) chain D
residue 59
type
sequence D
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

69) chain D
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

70) chain D
residue 90
type
sequence G
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

71) chain D
residue 91
type
sequence T
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

72) chain D
residue 92
type
sequence D
description BINDING SITE FOR RESIDUE GOL D 9004
source : BC3

73) chain A
residue 59
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

74) chain B
residue 271
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

75) chain C
residue 59
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

76) chain C
residue 91
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

77) chain C
residue 162
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

78) chain C
residue 240
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

79) chain C
residue 271
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

80) chain D
residue 59
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

81) chain D
residue 91
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

82) chain D
residue 162
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

83) chain D
residue 240
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

84) chain A
residue 91
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

85) chain D
residue 271
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

86) chain A
residue 162
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

87) chain A
residue 240
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

88) chain A
residue 271
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

89) chain B
residue 59
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

90) chain B
residue 91
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

91) chain B
residue 162
type BINDING
sequence T
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

92) chain B
residue 240
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:2P2N
source Swiss-Prot : SWS_FT_FI2

93) chain A
residue 14
type ACT_SITE
sequence T
description O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745
source Swiss-Prot : SWS_FT_FI1

94) chain B
residue 14
type ACT_SITE
sequence T
description O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745
source Swiss-Prot : SWS_FT_FI1

95) chain C
residue 14
type ACT_SITE
sequence T
description O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745
source Swiss-Prot : SWS_FT_FI1

96) chain D
residue 14
type ACT_SITE
sequence T
description O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745
source Swiss-Prot : SWS_FT_FI1

97) chain A
residue 8-16
type prosite
sequence VAYTGGTIG
description ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. VaYTGGTIG
source prosite : PS00144

98) chain A
residue 84-94
type prosite
sequence GFVILHGTDTM
description ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVilHGTDTM
source prosite : PS00917


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