eF-site ID 1fiq-ABC
PDB Code 1fiq
Chain A, B, C

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Title CRYSTAL STRUCTURE OF XANTHINE OXIDASE FROM BOVINE MILK
Classification OXIDOREDUCTASE
Compound XANTHINE OXIDASE
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence A:  TADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKL
GCGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLH
HVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIV
MSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFR
TFAK
B:  PKQLRFEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTE
IGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFGAAC
ALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVK
SVASLGGNIITASPISDLNPVFMASGTKLTIVSRGTRRTV
PMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQ
ASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRT
ISALKTTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGG
MIEFRRTLTLSFFFKFYLTVLKKLG
C:  DTVGRPLPHLAAAMQASGEAVYCDDIPRYENELFLRLVTS
TRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFN
DETVFAKDTVTCVGHIIGAVVADTPEHAERAAHVVKVTYE
DLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVV
SGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAM
KTQSFVAKMLGVPVNRILVRVKRMGGGFGGKETRSTLVSV
AVALAAYKTGHPVRCMLDRNEDMLITGGRHPFLARYKVGF
MKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYK
IPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEV
AVTCGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDE
CLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFT
VPFLNQAGALIHVYTDGSVLVSHGGTEMGQGLHTKMVQVA
SKALKIPISKIYISETSTNTVPNSSPTAASVSTDIYGQAV
YEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTT
GFYRTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGD
HKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEE
LHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNK
KAIYASKAVGEPPLFLGASVFFAIKDAIRAARAQHTNNNT
KELFRLDSPATPEKIRNACVDKFTT
Description


Functional site

1) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

2) chain A
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

3) chain A
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

4) chain A
residue 116
type
sequence C
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

5) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

6) chain A
residue 149
type
sequence R
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

7) chain A
residue 150
type
sequence C
description BINDING SITE FOR RESIDUE FES A 601
source : AC1

8) chain A
residue 42
type
sequence G
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

9) chain A
residue 43
type
sequence C
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

10) chain A
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

11) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

12) chain A
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

13) chain A
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

14) chain A
residue 49
type
sequence G
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

15) chain A
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

16) chain A
residue 71
type
sequence N
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

17) chain A
residue 73
type
sequence C
description BINDING SITE FOR RESIDUE FES A 602
source : AC2

18) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

19) chain A
residue 150
type
sequence C
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

20) chain C
residue 796
type
sequence G
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

21) chain C
residue 797
type
sequence G
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

22) chain C
residue 798
type
sequence F
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

23) chain C
residue 912
type
sequence R
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

24) chain C
residue 1038
type
sequence M
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

25) chain C
residue 1039
type
sequence G
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

26) chain C
residue 1040
type
sequence Q
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

27) chain C
residue 1078
type
sequence A
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

28) chain C
residue 1079
type
sequence A
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

29) chain C
residue 1080
type
sequence S
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

30) chain C
residue 1081
type
sequence V
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

31) chain C
residue 1082
type
sequence S
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

32) chain C
residue 1194
type
sequence Q
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

33) chain C
residue 1261
type
sequence E
description BINDING SITE FOR RESIDUE MTE C 1333
source : AC3

34) chain C
residue 767
type
sequence Q
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

35) chain C
residue 798
type
sequence F
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

36) chain C
residue 799
type
sequence G
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

37) chain C
residue 911
type
sequence F
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

38) chain C
residue 912
type
sequence R
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

39) chain C
residue 1078
type
sequence A
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

40) chain C
residue 1079
type
sequence A
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

41) chain C
residue 1261
type
sequence E
description BINDING SITE FOR RESIDUE MOS C 1334
source : AC4

42) chain C
residue 802
type
sequence E
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

43) chain C
residue 880
type
sequence R
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

44) chain C
residue 914
type
sequence F
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

45) chain C
residue 1008
type
sequence S
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

46) chain C
residue 1009
type
sequence F
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

47) chain C
residue 1010
type
sequence T
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

48) chain C
residue 1011
type
sequence V
description BINDING SITE FOR RESIDUE SAL C 1335
source : AC5

49) chain A
residue 45
type
sequence E
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

50) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

51) chain B
residue 256
type
sequence K
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

52) chain B
residue 257
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

53) chain B
residue 258
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

54) chain B
residue 259
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

55) chain B
residue 260
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

56) chain B
residue 261
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

57) chain B
residue 262
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

58) chain B
residue 263
type
sequence E
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

59) chain B
residue 264
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

60) chain B
residue 287
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

61) chain B
residue 337
type
sequence F
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

62) chain B
residue 338
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

63) chain B
residue 346
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

64) chain B
residue 347
type
sequence S
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

65) chain B
residue 350
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

66) chain B
residue 351
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

67) chain B
residue 353
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

68) chain B
residue 354
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

69) chain B
residue 359
type
sequence S
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

70) chain B
residue 360
type
sequence D
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

71) chain B
residue 404
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 606
source : AC6

72) chain C
residue 839
type
sequence R
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

73) chain C
residue 840
type
sequence H
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

74) chain C
residue 877
type
sequence I
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

75) chain C
residue 909
type
sequence T
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

76) chain C
residue 910
type
sequence A
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

77) chain C
residue 911
type
sequence F
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

78) chain C
residue 914
type
sequence F
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

79) chain C
residue 915
type
sequence G
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

80) chain C
residue 918
type
sequence Q
description BINDING SITE FOR RESIDUE GOL C 1336
source : AC7

81) chain C
residue 803
type catalytic
sequence T
description 139
source MCSA : MCSA1

82) chain C
residue 881
type catalytic
sequence A
description 139
source MCSA : MCSA1

83) chain C
residue 1262
type catalytic
sequence P
description 139
source MCSA : MCSA1

84) chain A
residue 43-51
type prosite
sequence CGEGGCGAC
description 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGEGGCGAC
source prosite : PS00197

85) chain C
residue 797-832
type prosite
sequence GFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNED
description MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD
source prosite : PS00559

86) chain C
residue 1262
type ACT_SITE
sequence P
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

87) chain B
residue 338
type ACT_SITE
sequence A
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

88) chain B
residue 348
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

89) chain B
residue 361
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

90) chain B
residue 405
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

91) chain B
residue 423
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

92) chain A
residue 148
type ACT_SITE
sequence C
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

93) chain A
residue 150
type ACT_SITE
sequence C
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

94) chain C
residue 768
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

95) chain C
residue 799
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

96) chain C
residue 913
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

97) chain C
residue 1080
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

98) chain C
residue 803
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

99) chain C
residue 881
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI3

100) chain C
residue 915
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI3

101) chain C
residue 1011
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3


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