eF-site ID 5vwq-ADGJ
PDB Code 5vwq
Chain A, D, G, J

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Title E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)
Classification TRANSFERASE
Compound Aspartate aminotransferase
Source Escherichia coli (strain K12) (AAT_ECOLI)
Sequence A:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET
GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE
LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD
ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR
ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR
MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
D:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET
GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE
LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD
ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR
ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR
MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
G:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET
GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE
LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD
ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR
ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR
MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
J:  MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDET
GKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE
LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD
ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIR
ANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR
MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Description


Functional site

1) chain A
residue 103
type
sequence G
description binding site for residue PMP A 401
source : AC1

2) chain A
residue 104
type
sequence T
description binding site for residue PMP A 401
source : AC1

3) chain A
residue 130
type
sequence W
description binding site for residue PMP A 401
source : AC1

4) chain A
residue 183
type
sequence N
description binding site for residue PMP A 401
source : AC1

5) chain A
residue 211
type
sequence D
description binding site for residue PMP A 401
source : AC1

6) chain A
residue 214
type
sequence Y
description binding site for residue PMP A 401
source : AC1

7) chain A
residue 243
type
sequence S
description binding site for residue PMP A 401
source : AC1

8) chain A
residue 245
type
sequence S
description binding site for residue PMP A 401
source : AC1

9) chain A
residue 246
type
sequence K
description binding site for residue PMP A 401
source : AC1

10) chain A
residue 254
type
sequence R
description binding site for residue PMP A 401
source : AC1

11) chain D
residue 65
type
sequence Y
description binding site for residue PMP A 401
source : AC1

12) chain A
residue 65
type
sequence Y
description binding site for residue PMP D 401
source : AC2

13) chain D
residue 103
type
sequence G
description binding site for residue PMP D 401
source : AC2

14) chain D
residue 104
type
sequence T
description binding site for residue PMP D 401
source : AC2

15) chain D
residue 130
type
sequence W
description binding site for residue PMP D 401
source : AC2

16) chain D
residue 183
type
sequence N
description binding site for residue PMP D 401
source : AC2

17) chain D
residue 211
type
sequence D
description binding site for residue PMP D 401
source : AC2

18) chain D
residue 214
type
sequence Y
description binding site for residue PMP D 401
source : AC2

19) chain D
residue 243
type
sequence S
description binding site for residue PMP D 401
source : AC2

20) chain D
residue 245
type
sequence S
description binding site for residue PMP D 401
source : AC2

21) chain D
residue 246
type
sequence K
description binding site for residue PMP D 401
source : AC2

22) chain D
residue 254
type
sequence R
description binding site for residue PMP D 401
source : AC2

23) chain G
residue 102
type
sequence G
description binding site for residue PMP G 401
source : AC3

24) chain G
residue 103
type
sequence G
description binding site for residue PMP G 401
source : AC3

25) chain G
residue 104
type
sequence T
description binding site for residue PMP G 401
source : AC3

26) chain G
residue 130
type
sequence W
description binding site for residue PMP G 401
source : AC3

27) chain G
residue 183
type
sequence N
description binding site for residue PMP G 401
source : AC3

28) chain G
residue 211
type
sequence D
description binding site for residue PMP G 401
source : AC3

29) chain G
residue 214
type
sequence Y
description binding site for residue PMP G 401
source : AC3

30) chain G
residue 243
type
sequence S
description binding site for residue PMP G 401
source : AC3

31) chain G
residue 245
type
sequence S
description binding site for residue PMP G 401
source : AC3

32) chain G
residue 246
type
sequence K
description binding site for residue PMP G 401
source : AC3

33) chain G
residue 254
type
sequence R
description binding site for residue PMP G 401
source : AC3

34) chain J
residue 65
type
sequence Y
description binding site for residue PMP G 401
source : AC3

35) chain G
residue 65
type
sequence Y
description binding site for residue PMP J 401
source : AC4

36) chain J
residue 102
type
sequence G
description binding site for residue PMP J 401
source : AC4

37) chain J
residue 103
type
sequence G
description binding site for residue PMP J 401
source : AC4

38) chain J
residue 104
type
sequence T
description binding site for residue PMP J 401
source : AC4

39) chain J
residue 130
type
sequence W
description binding site for residue PMP J 401
source : AC4

40) chain J
residue 183
type
sequence N
description binding site for residue PMP J 401
source : AC4

41) chain J
residue 211
type
sequence D
description binding site for residue PMP J 401
source : AC4

42) chain J
residue 214
type
sequence Y
description binding site for residue PMP J 401
source : AC4

43) chain J
residue 243
type
sequence S
description binding site for residue PMP J 401
source : AC4

44) chain J
residue 245
type
sequence S
description binding site for residue PMP J 401
source : AC4

45) chain J
residue 246
type
sequence K
description binding site for residue PMP J 401
source : AC4

46) chain J
residue 254
type
sequence R
description binding site for residue PMP J 401
source : AC4

47) chain A
residue 130
type catalytic
sequence W
description 777
source MCSA : MCSA1

48) chain A
residue 211
type catalytic
sequence D
description 777
source MCSA : MCSA1

49) chain A
residue 246
type catalytic
sequence K
description 777
source MCSA : MCSA1

50) chain D
residue 130
type catalytic
sequence W
description 777
source MCSA : MCSA2

51) chain D
residue 211
type catalytic
sequence D
description 777
source MCSA : MCSA2

52) chain D
residue 246
type catalytic
sequence K
description 777
source MCSA : MCSA2

53) chain G
residue 130
type catalytic
sequence W
description 777
source MCSA : MCSA3

54) chain G
residue 211
type catalytic
sequence D
description 777
source MCSA : MCSA3

55) chain G
residue 246
type catalytic
sequence K
description 777
source MCSA : MCSA3

56) chain J
residue 130
type catalytic
sequence W
description 777
source MCSA : MCSA4

57) chain J
residue 211
type catalytic
sequence D
description 777
source MCSA : MCSA4

58) chain J
residue 246
type catalytic
sequence K
description 777
source MCSA : MCSA4

59) chain A
residue 243-256
type prosite
sequence SYSKNFGLYNERVG
description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG
source prosite : PS00105

60) chain A
residue 34
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI1

61) chain D
residue 34
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI1

62) chain G
residue 34
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI1

63) chain J
residue 34
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 130
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI2

65) chain D
residue 130
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI2

66) chain G
residue 130
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI2

67) chain J
residue 130
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI2

68) chain A
residue 183
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI3

69) chain D
residue 183
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI3

70) chain G
residue 183
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI3

71) chain J
residue 183
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI3

72) chain A
residue 374
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI4

73) chain D
residue 374
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI4

74) chain G
residue 374
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI4

75) chain J
residue 374
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
source Swiss-Prot : SWS_FT_FI4

76) chain A
residue 246
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA
source Swiss-Prot : SWS_FT_FI5

77) chain D
residue 246
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA
source Swiss-Prot : SWS_FT_FI5

78) chain G
residue 246
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA
source Swiss-Prot : SWS_FT_FI5

79) chain J
residue 246
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA
source Swiss-Prot : SWS_FT_FI5


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