eF-site ID 2xij-A
PDB Code 2xij
Chain A

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Title Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin
Classification ISOMERASE
Compound METHYLMALONYL-COA MUTASE, MITOCHONDRIAL
Source Homo sapiens (Human) (MUTA_HUMAN)
Sequence A:  QQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSK
RDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFST
VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRG
DVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV
LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP
EPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL
ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNF
YMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSG
WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALG
LPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT
NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARR
QARIDSGSEVIVGVNKYQLEKEDTVEVLAIDNTSVRNRQI
EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDA
SRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK
EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIA
TGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLA
AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFE
VGVSNVFGPGTRIPKAAVQVLDDIEKCLEK
Description


Functional site

1) chain A
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

2) chain A
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

3) chain A
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

4) chain A
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

5) chain A
residue 227
type
sequence V
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

6) chain A
residue 228
type
sequence R
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

7) chain A
residue 230
type
sequence T
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

8) chain A
residue 268
type
sequence E
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

9) chain A
residue 356
type
sequence W
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

10) chain A
residue 392
type
sequence E
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

11) chain A
residue 393
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

12) chain A
residue 394
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

13) chain A
residue 395
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

14) chain A
residue 476
type
sequence Q
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

15) chain A
residue 626
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

16) chain A
residue 627
type
sequence H
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

17) chain A
residue 628
type
sequence D
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

18) chain A
residue 629
type
sequence R
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

19) chain A
residue 630
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

20) chain A
residue 634
type
sequence I
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

21) chain A
residue 670
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

22) chain A
residue 672
type
sequence S
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

23) chain A
residue 674
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

24) chain A
residue 675
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

25) chain A
residue 676
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

26) chain A
residue 702
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

27) chain A
residue 703
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

28) chain A
residue 704
type
sequence V
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

29) chain A
residue 722
type
sequence F
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

30) chain A
residue 723
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

31) chain A
residue 724
type
sequence P
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

32) chain A
residue 726
type
sequence T
description BINDING SITE FOR RESIDUE B12 A 800
source : AC1

33) chain A
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE 5AD A 1746
source : AC2

34) chain A
residue 352
type
sequence Q
description BINDING SITE FOR RESIDUE 5AD A 1746
source : AC2

35) chain A
residue 396
type
sequence L
description BINDING SITE FOR RESIDUE 5AD A 1746
source : AC2

36) chain A
residue 613
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

37) chain A
residue 613
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

38) chain A
residue 614
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

39) chain A
residue 614
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

40) chain A
residue 616
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

41) chain A
residue 616
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1747
source : AC3

42) chain A
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 A 1748
source : AC4

43) chain A
residue 150
type
sequence N
description BINDING SITE FOR RESIDUE SO4 A 1748
source : AC4

44) chain A
residue 152
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 1748
source : AC4

45) chain A
residue 594
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1749
source : AC5

46) chain A
residue 595
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1749
source : AC5

47) chain A
residue 596
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 1749
source : AC5

48) chain A
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 1750
source : AC6

49) chain A
residue 272
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 1750
source : AC6

50) chain A
residue 274
type
sequence I
description BINDING SITE FOR RESIDUE EDO A 1750
source : AC6

51) chain A
residue 58
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 1751
source : AC7

52) chain A
residue 60
type
sequence I
description BINDING SITE FOR RESIDUE EDO A 1751
source : AC7

53) chain A
residue 61
type
sequence W
description BINDING SITE FOR RESIDUE EDO A 1751
source : AC7

54) chain A
residue 420
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1751
source : AC7

55) chain A
residue 108
type
sequence R
description BINDING SITE FOR RESIDUE EDO A 1752
source : AC8

56) chain A
residue 306
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1752
source : AC8

57) chain A
residue 350
type
sequence H
description BINDING SITE FOR RESIDUE EDO A 1752
source : AC8

58) chain A
residue 384
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1752
source : AC8

59) chain A
residue 249
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1757
source : AC9

60) chain A
residue 250
type
sequence A
description BINDING SITE FOR RESIDUE EDO A 1757
source : AC9

61) chain A
residue 258
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1757
source : AC9

62) chain A
residue 304
type
sequence R
description BINDING SITE FOR RESIDUE EDO A 1757
source : AC9

63) chain A
residue 117
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 1753
source : BC1

64) chain A
residue 510
type
sequence V
description BINDING SITE FOR RESIDUE EDO A 1753
source : BC1

65) chain A
residue 514
type
sequence Q
description BINDING SITE FOR RESIDUE EDO A 1753
source : BC1

66) chain A
residue 517
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1753
source : BC1

67) chain A
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

68) chain A
residue 185
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

69) chain A
residue 186
type
sequence M
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

70) chain A
residue 216
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

71) chain A
residue 218
type
sequence Q
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

72) chain A
residue 260
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

73) chain A
residue 308
type
sequence F
description BINDING SITE FOR RESIDUE EDO A 1754
source : BC2

74) chain A
residue 695
type
sequence P
description BINDING SITE FOR RESIDUE EDO A 1755
source : BC3

75) chain A
residue 697
type
sequence I
description BINDING SITE FOR RESIDUE EDO A 1755
source : BC3

76) chain A
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

77) chain A
residue 108
type
sequence R
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

78) chain A
residue 109
type
sequence Q
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

79) chain A
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

80) chain A
residue 111
type
sequence A
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

81) chain A
residue 131
type
sequence Q
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

82) chain A
residue 135
type
sequence S
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

83) chain A
residue 406
type
sequence R
description BINDING SITE FOR RESIDUE BTB A 1756
source : BC4

84) chain A
residue 627
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI2

85) chain A
residue 89
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

86) chain A
residue 212
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

87) chain A
residue 335
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

88) chain A
residue 602
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

89) chain A
residue 343
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

90) chain A
residue 595
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

91) chain A
residue 50
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

92) chain A
residue 96
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

93) chain A
residue 106
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

94) chain A
residue 216
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

95) chain A
residue 228
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

96) chain A
residue 255
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

97) chain A
residue 265
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

98) chain A
residue 304
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

99) chain A
residue 481
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

100) chain A
residue 403-428
type prosite
sequence RIARNTQIIIQEESGIPKVADPWGGS
description METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS
source prosite : PS00544


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