eF-site ID 4wr3-ABCD
PDB Code 4wr3
Chain A, B, C, D

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Title Y274F alanine racemase from E. coli
Classification ISOMERASE
Compound Alanine racemase, biosynthetic
Source Escherichia coli (strain K12) (ALR1_ECOLI)
Sequence A:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH
GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG
FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW
MKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF
ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW
PQSHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSS
LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGFGDGYPR
AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD
PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
B:  QAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHG
LLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGF
FDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWM
KLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFA
RADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWP
QSHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSL
IAVREHKAGEPVGYGGTWVSERDTRLGVVAMGFGDGYPRA
APSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDP
VILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
C:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL
LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF
DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMK
LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR
ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ
SHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLI
AVREHKAGEPVGYGGTWVSERDTRLGVVAMGFGDGYPRAA
PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV
ILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
D:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL
LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF
DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMK
LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR
ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ
SHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLI
AVREHKAGEPVGYGGTWVSERDTRLGVVAMGFGDGYPRAA
PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV
ILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
Description


Functional site

1) chain A
residue 38
type
sequence Y
description binding site for residue PLP A 1001
source : AC1

2) chain A
residue 159
type
sequence H
description binding site for residue PLP A 1001
source : AC1

3) chain A
residue 193
type
sequence A
description binding site for residue PLP A 1001
source : AC1

4) chain A
residue 194
type
sequence S
description binding site for residue PLP A 1001
source : AC1

5) chain A
residue 209
type
sequence R
description binding site for residue PLP A 1001
source : AC1

6) chain A
residue 211
type
sequence G
description binding site for residue PLP A 1001
source : AC1

7) chain A
residue 212
type
sequence I
description binding site for residue PLP A 1001
source : AC1

8) chain A
residue 343
type
sequence Y
description binding site for residue PLP A 1001
source : AC1

9) chain A
residue 129
type
sequence R
description binding site for residue SO4 A 1002
source : AC2

10) chain A
residue 130
type
sequence L
description binding site for residue SO4 A 1002
source : AC2

11) chain A
residue 159
type
sequence H
description binding site for residue SO4 A 1002
source : AC2

12) chain A
residue 266
type
sequence R
description binding site for residue SO4 A 1003
source : AC3

13) chain B
residue 19
type
sequence R
description binding site for residue SO4 A 1003
source : AC3

14) chain A
residue 255
type
sequence Y
description binding site for residue GOL A 1004
source : AC4

15) chain A
residue 302
type
sequence A
description binding site for residue GOL A 1004
source : AC4

16) chain A
residue 303
type
sequence M
description binding site for residue GOL A 1004
source : AC4

17) chain A
residue 304
type
sequence D
description binding site for residue GOL A 1004
source : AC4

18) chain B
residue 129
type
sequence R
description binding site for residue GOL A 1004
source : AC4

19) chain B
residue 38
type
sequence Y
description binding site for residue PLP B 1001
source : AC5

20) chain B
residue 159
type
sequence H
description binding site for residue PLP B 1001
source : AC5

21) chain B
residue 193
type
sequence A
description binding site for residue PLP B 1001
source : AC5

22) chain B
residue 194
type
sequence S
description binding site for residue PLP B 1001
source : AC5

23) chain B
residue 209
type
sequence R
description binding site for residue PLP B 1001
source : AC5

24) chain B
residue 211
type
sequence G
description binding site for residue PLP B 1001
source : AC5

25) chain B
residue 212
type
sequence I
description binding site for residue PLP B 1001
source : AC5

26) chain B
residue 343
type
sequence Y
description binding site for residue PLP B 1001
source : AC5

27) chain B
residue 129
type
sequence R
description binding site for residue SO4 B 1002
source : AC6

28) chain B
residue 130
type
sequence L
description binding site for residue SO4 B 1002
source : AC6

29) chain B
residue 159
type
sequence H
description binding site for residue SO4 B 1002
source : AC6

30) chain A
residue 19
type
sequence R
description binding site for residue SO4 B 1003
source : AC7

31) chain B
residue 266
type
sequence R
description binding site for residue SO4 B 1003
source : AC7

32) chain A
residue 129
type
sequence R
description binding site for residue GOL B 1004
source : AC8

33) chain B
residue 255
type
sequence Y
description binding site for residue GOL B 1004
source : AC8

34) chain B
residue 302
type
sequence A
description binding site for residue GOL B 1004
source : AC8

35) chain B
residue 303
type
sequence M
description binding site for residue GOL B 1004
source : AC8

36) chain B
residue 304
type
sequence D
description binding site for residue GOL B 1004
source : AC8

37) chain B
residue 305
type
sequence M
description binding site for residue GOL B 1004
source : AC8

38) chain C
residue 38
type
sequence Y
description binding site for residue PLP C 1001
source : AC9

39) chain C
residue 193
type
sequence A
description binding site for residue PLP C 1001
source : AC9

40) chain C
residue 194
type
sequence S
description binding site for residue PLP C 1001
source : AC9

41) chain C
residue 209
type
sequence R
description binding site for residue PLP C 1001
source : AC9

42) chain C
residue 211
type
sequence G
description binding site for residue PLP C 1001
source : AC9

43) chain C
residue 212
type
sequence I
description binding site for residue PLP C 1001
source : AC9

44) chain C
residue 343
type
sequence Y
description binding site for residue PLP C 1001
source : AC9

45) chain C
residue 19
type
sequence R
description binding site for residue SO4 C 1002
source : AD1

46) chain D
residue 266
type
sequence R
description binding site for residue SO4 C 1002
source : AD1

47) chain D
residue 38
type
sequence Y
description binding site for residue PLP D 1001
source : AD2

48) chain D
residue 193
type
sequence A
description binding site for residue PLP D 1001
source : AD2

49) chain D
residue 194
type
sequence S
description binding site for residue PLP D 1001
source : AD2

50) chain D
residue 209
type
sequence R
description binding site for residue PLP D 1001
source : AD2

51) chain D
residue 211
type
sequence G
description binding site for residue PLP D 1001
source : AD2

52) chain D
residue 212
type
sequence I
description binding site for residue PLP D 1001
source : AD2

53) chain D
residue 343
type
sequence Y
description binding site for residue PLP D 1001
source : AD2

54) chain C
residue 129
type
sequence R
description binding site for residue GOL D 1002
source : AD3

55) chain D
residue 255
type
sequence Y
description binding site for residue GOL D 1002
source : AD3

56) chain D
residue 302
type
sequence A
description binding site for residue GOL D 1002
source : AD3

57) chain D
residue 303
type
sequence M
description binding site for residue GOL D 1002
source : AD3

58) chain D
residue 304
type
sequence D
description binding site for residue GOL D 1002
source : AD3

59) chain D
residue 305
type
sequence M
description binding site for residue GOL D 1002
source : AD3

60) chain A
residue 34
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

61) chain B
residue 34
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

62) chain C
residue 34
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

63) chain D
residue 34
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 255
type ACT_SITE
sequence Y
description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI2

65) chain B
residue 255
type ACT_SITE
sequence Y
description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI2

66) chain C
residue 255
type ACT_SITE
sequence Y
description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI2

67) chain D
residue 255
type ACT_SITE
sequence Y
description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI2

68) chain A
residue 129
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

69) chain A
residue 303
type BINDING
sequence M
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

70) chain B
residue 129
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

71) chain B
residue 303
type BINDING
sequence M
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

72) chain C
residue 129
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

73) chain C
residue 303
type BINDING
sequence M
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

74) chain D
residue 129
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

75) chain D
residue 303
type BINDING
sequence M
description BINDING => ECO:0000305|PubMed:18434499
source Swiss-Prot : SWS_FT_FI3

76) chain A
residue 34
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI4

77) chain B
residue 34
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI4

78) chain C
residue 34
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI4

79) chain D
residue 34
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI4

80) chain A
residue 122
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI5

81) chain B
residue 122
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI5

82) chain C
residue 122
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI5

83) chain D
residue 122
type MOD_RES
sequence K
description N6-carboxylysine => ECO:0000269|PubMed:18434499
source Swiss-Prot : SWS_FT_FI5

84) chain A
residue 31-41
type prosite
sequence AVVKANAYGHG
description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG
source prosite : PS00395


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