eF-site ID 3b8u-ABCD
PDB Code 3b8u
Chain A, B, C, D

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Title Crystal structure of Escherichia coli alaine racemase mutant E221A
Classification ISOMERASE
Compound Alanine racemase
Source Escherichia coli (strain K12) (ALR1_ECOLI)
Sequence A:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH
GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG
FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW
MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF
ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW
PQSHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSS
LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR
AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD
PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
B:  QAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHG
LLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGF
FDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWM
XLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFA
RADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWP
QSHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSSL
IAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRA
APSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDP
VILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD
C:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL
LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF
DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX
LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR
ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ
SHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSSLI
AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA
PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV
ILWLPVERIKVSAYELITRLTSRVAMKYVD
D:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL
LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF
DARDLPTISAQHFHTAVHNEEQLAALEEALDEPVTVWMXL
DTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFARA
DEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQS
HFDWVRPGIILYGVSPLSTGADFGCQPVMSLTSSLIAVRE
HKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGT
PVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPVILWG
EGLPVERIKVSAYELITRLTSRVAMKYVD
Description


Functional site

1) chain A
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 360
source : AC1

2) chain A
residue 274
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 360
source : AC1

3) chain A
residue 280
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 360
source : AC1

4) chain A
residue 19
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 361
source : AC2

5) chain B
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 361
source : AC2

6) chain B
residue 315
type
sequence Q
description BINDING SITE FOR RESIDUE SO4 A 361
source : AC2

7) chain B
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 B 360
source : AC3

8) chain B
residue 274
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 B 360
source : AC3

9) chain B
residue 280
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 360
source : AC3

10) chain A
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 361
source : AC4

11) chain B
residue 19
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 361
source : AC4

12) chain B
residue 162
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 362
source : AC5

13) chain C
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 C 360
source : AC6

14) chain C
residue 274
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 C 360
source : AC6

15) chain C
residue 280
type
sequence R
description BINDING SITE FOR RESIDUE SO4 C 360
source : AC6

16) chain C
residue 302
type
sequence A
description BINDING SITE FOR RESIDUE SO4 C 360
source : AC6

17) chain C
residue 19
type
sequence R
description BINDING SITE FOR RESIDUE SO4 C 361
source : AC7

18) chain D
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE SO4 C 361
source : AC7

19) chain C
residue 343
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 D 360
source : AC8

20) chain D
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 D 360
source : AC8

21) chain D
residue 274
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 D 360
source : AC8

22) chain D
residue 280
type
sequence R
description BINDING SITE FOR RESIDUE SO4 D 360
source : AC8

23) chain C
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE SO4 D 361
source : AC9

24) chain D
residue 19
type
sequence R
description BINDING SITE FOR RESIDUE SO4 D 361
source : AC9

25) chain A
residue 34
type
sequence K
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

26) chain A
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

27) chain A
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

28) chain A
residue 193
type
sequence A
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

29) chain A
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

30) chain A
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

31) chain A
residue 211
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

32) chain A
residue 212
type
sequence I
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

33) chain A
residue 343
type
sequence Y
description BINDING SITE FOR RESIDUE PLP A 1001
source : BC1

34) chain B
residue 34
type
sequence K
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

35) chain B
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

36) chain B
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

37) chain B
residue 193
type
sequence A
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

38) chain B
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

39) chain B
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

40) chain B
residue 211
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

41) chain B
residue 212
type
sequence I
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

42) chain B
residue 343
type
sequence Y
description BINDING SITE FOR RESIDUE PLP B 1001
source : BC2

43) chain C
residue 34
type
sequence K
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

44) chain C
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

45) chain C
residue 78
type
sequence L
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

46) chain C
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

47) chain C
residue 193
type
sequence A
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

48) chain C
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

49) chain C
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

50) chain C
residue 211
type
sequence G
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

51) chain C
residue 212
type
sequence I
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

52) chain C
residue 343
type
sequence Y
description BINDING SITE FOR RESIDUE PLP C 1001
source : BC3

53) chain D
residue 34
type
sequence K
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

54) chain D
residue 38
type
sequence Y
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

55) chain D
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

56) chain D
residue 193
type
sequence A
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

57) chain D
residue 194
type
sequence S
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

58) chain D
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

59) chain D
residue 211
type
sequence G
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

60) chain D
residue 212
type
sequence I
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

61) chain D
residue 343
type
sequence Y
description BINDING SITE FOR RESIDUE PLP D 1001
source : BC4

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

63) 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

64) 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

65) 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

66) 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

67) 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

68) 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

69) 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

70) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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