eF-site ID 6d5k-ABC
PDB Code 6d5k
Chain A, B, C

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Title Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, and Adenosylcobalamin
Classification TRANSFERASE
Compound Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial
Source (MMAB_HUMAN)
Sequence A:  DDQVFEAVGTTDELSSAIGFALELVTEKGHTFAEELQKIQ
CTLQDVGSALATKYTTFKAGPILELEQWIDKYTSQLPPLT
AFILPSGGKISSALHFCRAVCRRAERRVVPLVQMGETDAN
VAKFLNRLSDYLFTLARYAAMKEGNQEKIYMK
B:  KIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAI
GFALELVTEKGHTFAEELQKIQCTLQDVGSALATPCSSAR
EAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGG
KISSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRL
SDYLFTLARYAAMKEGNQEKIY
C:  DKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFALELV
TEKGHTFAEELQKIQCTLQDVGSALATPCSSAREAHLKYT
TFKAGPILELEQWIDKYTSQLPPLTAFILPSGGKISSALH
FCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTL
ARYAAMKEGNQEKIYMKN
Description


Functional site

1) chain A
residue 190
type
sequence R
description binding site for residue 5AD A 301
source : AC1

2) chain A
residue 193
type
sequence E
description binding site for residue 5AD A 301
source : AC1

3) chain A
residue 194
type
sequence R
description binding site for residue 5AD A 301
source : AC1

4) chain C
residue 68
type
sequence S
description binding site for residue 5AD A 301
source : AC1

5) chain C
residue 69
type
sequence S
description binding site for residue 5AD A 301
source : AC1

6) chain C
residue 78
type
sequence K
description binding site for residue 5AD A 301
source : AC1

7) chain C
residue 83
type
sequence F
description binding site for residue 5AD A 301
source : AC1

8) chain A
residue 168
type
sequence T
description binding site for residue B12 A 302
source : AC2

9) chain A
residue 169
type
sequence A
description binding site for residue B12 A 302
source : AC2

10) chain A
residue 170
type
sequence F
description binding site for residue B12 A 302
source : AC2

11) chain A
residue 171
type
sequence I
description binding site for residue B12 A 302
source : AC2

12) chain A
residue 186
type
sequence R
description binding site for residue B12 A 302
source : AC2

13) chain A
residue 190
type
sequence R
description binding site for residue B12 A 302
source : AC2

14) chain A
residue 217
type
sequence S
description binding site for residue B12 A 302
source : AC2

15) chain A
residue 218
type
sequence D
description binding site for residue B12 A 302
source : AC2

16) chain A
residue 221
type
sequence F
description binding site for residue B12 A 302
source : AC2

17) chain A
residue 239
type
sequence M
description binding site for residue B12 A 302
source : AC2

18) chain C
residue 71
type
sequence F
description binding site for residue B12 A 302
source : AC2

19) chain C
residue 86
type
sequence V
description binding site for residue B12 A 302
source : AC2

20) chain C
residue 90
type
sequence D
description binding site for residue B12 A 302
source : AC2

21) chain C
residue 122
type
sequence Q
description binding site for residue B12 A 302
source : AC2

22) chain C
residue 126
type
sequence S
description binding site for residue B12 A 302
source : AC2

23) chain C
residue 129
type
sequence A
description binding site for residue B12 A 302
source : AC2

24) chain A
residue 86
type
sequence V
description binding site for residue B12 A 303
source : AC3

25) chain A
residue 90
type
sequence D
description binding site for residue B12 A 303
source : AC3

26) chain A
residue 122
type
sequence Q
description binding site for residue B12 A 303
source : AC3

27) chain A
residue 126
type
sequence S
description binding site for residue B12 A 303
source : AC3

28) chain B
residue 57
type
sequence K
description binding site for residue B12 A 303
source : AC3

29) chain B
residue 167
type
sequence L
description binding site for residue B12 A 303
source : AC3

30) chain B
residue 168
type
sequence T
description binding site for residue B12 A 303
source : AC3

31) chain B
residue 170
type
sequence F
description binding site for residue B12 A 303
source : AC3

32) chain B
residue 171
type
sequence I
description binding site for residue B12 A 303
source : AC3

33) chain B
residue 186
type
sequence R
description binding site for residue B12 A 303
source : AC3

34) chain B
residue 190
type
sequence R
description binding site for residue B12 A 303
source : AC3

35) chain B
residue 217
type
sequence S
description binding site for residue B12 A 303
source : AC3

36) chain B
residue 221
type
sequence F
description binding site for residue B12 A 303
source : AC3

37) chain A
residue 108
type
sequence H
description binding site for residue SO4 A 304
source : AC4

38) chain A
residue 109
type
sequence T
description binding site for residue SO4 A 304
source : AC4

39) chain A
residue 110
type
sequence F
description binding site for residue SO4 A 304
source : AC4

40) chain A
residue 226
type
sequence Y
description binding site for residue SO4 A 304
source : AC4

41) chain A
residue 83
type
sequence F
description binding site for residue 5AD B 301
source : AC5

42) chain B
residue 190
type
sequence R
description binding site for residue 5AD B 301
source : AC5

43) chain B
residue 193
type
sequence E
description binding site for residue 5AD B 301
source : AC5

44) chain B
residue 194
type
sequence R
description binding site for residue 5AD B 301
source : AC5

45) chain B
residue 108
type
sequence H
description binding site for residue SO4 B 302
source : AC6

46) chain B
residue 109
type
sequence T
description binding site for residue SO4 B 302
source : AC6

47) chain B
residue 110
type
sequence F
description binding site for residue SO4 B 302
source : AC6

48) chain B
residue 226
type
sequence Y
description binding site for residue SO4 B 302
source : AC6

49) chain B
residue 211
type
sequence K
description binding site for residue SO4 B 303
source : AC7

50) chain C
residue 141
type
sequence K
description binding site for residue SO4 B 303
source : AC7

51) chain C
residue 142
type
sequence Y
description binding site for residue SO4 B 303
source : AC7

52) chain B
residue 60
type
sequence T
description binding site for residue ATP C 301
source : AC8

53) chain B
residue 61
type
sequence K
description binding site for residue ATP C 301
source : AC8

54) chain B
residue 62
type
sequence T
description binding site for residue ATP C 301
source : AC8

55) chain B
residue 63
type
sequence G
description binding site for residue ATP C 301
source : AC8

56) chain B
residue 68
type
sequence S
description binding site for residue ATP C 301
source : AC8

57) chain B
residue 69
type
sequence S
description binding site for residue ATP C 301
source : AC8

58) chain B
residue 78
type
sequence K
description binding site for residue ATP C 301
source : AC8

59) chain B
residue 83
type
sequence F
description binding site for residue ATP C 301
source : AC8

60) chain C
residue 190
type
sequence R
description binding site for residue ATP C 301
source : AC8

61) chain C
residue 193
type
sequence E
description binding site for residue ATP C 301
source : AC8

62) chain C
residue 194
type
sequence R
description binding site for residue ATP C 301
source : AC8

63) chain C
residue 214
type
sequence N
description binding site for residue ATP C 301
source : AC8

64) chain B
residue 58
type
sequence I
description binding site for residue MG C 302
source : AC9

65) chain C
residue 218
type
sequence D
description binding site for residue MG C 302
source : AC9

66) chain A
residue 214
type
sequence N
description binding site for residue EPE C 303
source : AD1

67) chain A
residue 218
type
sequence D
description binding site for residue EPE C 303
source : AD1

68) chain C
residue 68
type
sequence S
description binding site for residue EPE C 303
source : AD1

69) chain C
residue 69
type
sequence S
description binding site for residue EPE C 303
source : AD1

70) chain C
residue 75
type
sequence R
description binding site for residue EPE C 303
source : AD1

71) chain C
residue 108
type
sequence H
description binding site for residue SO4 C 304
source : AD2

72) chain C
residue 109
type
sequence T
description binding site for residue SO4 C 304
source : AD2

73) chain C
residue 110
type
sequence F
description binding site for residue SO4 C 304
source : AD2

74) chain C
residue 226
type
sequence Y
description binding site for residue SO4 C 304
source : AD2

75) chain C
residue 230
type
sequence K
description binding site for residue SO4 C 304
source : AD2

76) chain C
residue 147
type
sequence A
description binding site for residue SO4 C 305
source : AD3

77) chain C
residue 208
type
sequence N
description binding site for residue SO4 C 305
source : AD3

78) chain C
residue 214
type
sequence N
description binding site for residue MG C 306
source : AD4

79) chain B
residue 214
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

80) chain C
residue 68
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

81) chain C
residue 78
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

82) chain C
residue 190
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

83) chain C
residue 214
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

84) chain A
residue 190
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

85) chain A
residue 214
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

86) chain B
residue 60
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

87) chain B
residue 68
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

88) chain B
residue 78
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

89) chain B
residue 190
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17176040
source Swiss-Prot : SWS_FT_FI1

90) chain B
residue 134
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI2

91) chain C
residue 134
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI2

92) chain B
residue 211
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI3

93) chain C
residue 211
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI3

94) chain A
residue 211
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI3

95) chain B
residue 230
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI4

96) chain C
residue 230
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI4

97) chain A
residue 230
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D273
source Swiss-Prot : SWS_FT_FI4


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