eF-site ID 1xkv-AB
PDB Code 1xkv
Chain A, B

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Title Crystal Structure Of ATP-Dependent Phosphoenolpyruvate Carboxykinase From Thermus thermophilus HB8
Classification LYASE
Compound ATP-dependent phosphoenolpyruvate carboxykinase
Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (Q5SLL5_THET8)
Sequence A:  QRLEALGIHPKKRVFWNTVSPVLVEHTLLRGEGLLAHHGP
LVVDTTPYTGRSPKDKFVVREPEVEGEIWWGEVNQPFAPE
AFEALYQRVVQYLSERDLYVQDLYAGADRRYRLAVRVVTE
SPWHALFARNMFILPRRFGAFVPGFTVVHAPYFQAVPERD
GTRSEVFVGISFQRRLVLIVGTKYAGEIKKSIFTVMNYLM
PKRGVFPMHASANVGKEGDVAVFFGLSGTGKTTLSTDPER
PLIGDDEHGWSEDGVFNFEGGCYAKVIRLSPEHEPLIYKA
SNQFEAILENVVVNPESRRVQWDDDSKTENTRSSYPIAHL
ENVVESGVAGHPRAIFFLSADAYGVLPPIARLSPEEAMYY
FLSGYTARVTEPRATFSACFGAPFLPMHPGVYARMLGEKI
RKHAPRVYLVNTGWTGGPYGVGYRFPLPVTRALLKAALSG
ALENVPYRRDPVFGFEVPLEAPGVPQELLNPRETWADKEA
YDQQARKLARLFQENFQKYASGVAKEVAEAGPRTE
B:  MQRLEALGIHPKKRVFWNTVSPVLVEHTLLRGEGLLAHHG
PLVVDTTPYTGRSPKDKFVVREPEVEGEIWWGEVNQPFAP
EAFEALYQRVVQYLSERDLYVQDLYAGADRRYRLAVRVVT
ESPWHALFARNMFILPRRFGNDDEVEAFVPGFTVVHAPYF
QAVPERDGTRSEVFVGISFQRRLVLIVGTKYAGEIKKSIF
TVMNYLMPKRGVFPMHASANVGKEGDVAVFFGLSGTGKTT
LSTDPERPLIGDDEHGWSEDGVFNFEGGCYAKVIRLSPEH
EPLIYKASNQFEAILENVVVNPESRRVQWDDDSKTENTRS
SYPIAHLENVVESGVAGHPRAIFFLSADAYGVLPPIARLS
PEEAMYYFLSGYTARVPRATFSACFGAPFLPMHPGVYARM
LGEKIRKHAPRVYLVNTGWTGGPYGVGYRFPLPVTRALLK
AALSGALENVPYRRDPVFGFEVPLEAPGVPQELLNPRETW
ADKEAYDQQARKLARLFQENFQKYASGVAKEVAEAGPRT
Description


Functional site

1) chain A
residue 130
type
sequence R
description BINDING SITE FOR RESIDUE CA A 2001
source : AC1

2) chain A
residue 131
type
sequence N
description BINDING SITE FOR RESIDUE CA A 2001
source : AC1

3) chain A
residue 133
type
sequence F
description BINDING SITE FOR RESIDUE CA A 2001
source : AC1

4) chain A
residue 267
type
sequence G
description BINDING SITE FOR RESIDUE CA A 2001
source : AC1

5) chain B
residue 130
type
sequence R
description BINDING SITE FOR RESIDUE CA B 2002
source : AC2

6) chain B
residue 131
type
sequence N
description BINDING SITE FOR RESIDUE CA B 2002
source : AC2

7) chain B
residue 133
type
sequence F
description BINDING SITE FOR RESIDUE CA B 2002
source : AC2

8) chain B
residue 267
type
sequence G
description BINDING SITE FOR RESIDUE CA B 2002
source : AC2

9) chain A
residue 20
type
sequence V
description BINDING SITE FOR RESIDUE PO4 A 3001
source : AC3

10) chain A
residue 21
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 3001
source : AC3

11) chain A
residue 130
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 3001
source : AC3

12) chain A
residue 137
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 3001
source : AC3

13) chain B
residue 38
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 3001
source : AC3

14) chain A
residue 259
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 3002
source : AC4

15) chain A
residue 413
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 3002
source : AC4

16) chain A
residue 416
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 3002
source : AC4

17) chain A
residue 417
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 3002
source : AC4

18) chain A
residue 38
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 3003
source : AC5

19) chain B
residue 21
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 3003
source : AC5

20) chain B
residue 22
type
sequence P
description BINDING SITE FOR RESIDUE PO4 B 3003
source : AC5

21) chain B
residue 130
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 3003
source : AC5

22) chain B
residue 137
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 3003
source : AC5

23) chain B
residue 413
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3004
source : AC6

24) chain B
residue 416
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3004
source : AC6

25) chain B
residue 417
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 3004
source : AC6

26) chain B
residue 233
type
sequence L
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

27) chain B
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

28) chain B
residue 235
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

29) chain B
residue 236
type
sequence T
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

30) chain B
residue 237
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

31) chain B
residue 238
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

32) chain B
residue 239
type
sequence T
description BINDING SITE FOR RESIDUE PO4 B 3005
source : AC7

33) chain B
residue 5
type
sequence E
description BINDING SITE FOR RESIDUE PO4 B 3006
source : AC8

34) chain B
residue 10
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 3006
source : AC8

35) chain B
residue 12
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 3006
source : AC8

36) chain A
residue 233
type
sequence L
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

37) chain A
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

38) chain A
residue 235
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

39) chain A
residue 236
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

40) chain A
residue 237
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

41) chain A
residue 238
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

42) chain A
residue 239
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

43) chain A
residue 240
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

44) chain A
residue 272
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

45) chain A
residue 426
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

46) chain A
residue 438
type
sequence R
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

47) chain A
residue 439
type
sequence F
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

48) chain A
residue 444
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1001
source : AC9

49) chain B
residue 160
type
sequence F
description BINDING SITE FOR RESIDUE GOL B 4001
source : BC1

50) chain B
residue 161
type
sequence Q
description BINDING SITE FOR RESIDUE GOL B 4001
source : BC1

51) chain B
residue 166
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 4001
source : BC1

52) chain A
residue 66
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

53) chain A
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

54) chain A
residue 71
type
sequence W
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

55) chain B
residue 50
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

56) chain B
residue 51
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

57) chain B
residue 315
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 4002
source : BC2

58) chain A
residue 52
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

59) chain B
residue 253
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

60) chain B
residue 281
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

61) chain B
residue 319
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

62) chain A
residue 191
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 197
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 253
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 281
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 319
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

67) chain B
residue 52
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

68) chain B
residue 191
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

69) chain B
residue 197
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453
source Swiss-Prot : SWS_FT_FI1

70) chain A
residue 130
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 131
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

72) chain A
residue 267
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

73) chain B
residue 130
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

74) chain B
residue 131
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

75) chain B
residue 267
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI2

76) chain A
residue 133
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI3

77) chain B
residue 133
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI3

78) chain A
residue 216
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P22259
source Swiss-Prot : SWS_FT_FI4

79) chain B
residue 216
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P22259
source Swiss-Prot : SWS_FT_FI4

80) chain A
residue 438
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:16239727, ECO:0000305|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI6

81) chain B
residue 438
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:16239727, ECO:0000305|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI6

82) chain A
residue 439
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3
source Swiss-Prot : SWS_FT_FI7

83) chain B
residue 439
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3
source Swiss-Prot : SWS_FT_FI7

84) chain A
residue 249-264
type prosite
sequence LIGDDEHGWSEDGVFN
description PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWsEdGVfN
source prosite : PS00532

85) chain A
residue 232
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI5

86) chain A
residue 444
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI5

87) chain B
residue 232
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI5

88) chain B
residue 444
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9
source Swiss-Prot : SWS_FT_FI5


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