eF-site ID 1fo4-A
PDB Code 1fo4
Chain A

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Title CRYSTAL STRUCTURE OF XANTHINE DEHYDROGENASE ISOLATED FROM BOVINE MILK
Classification OXIDOREDUCTASE
Compound XANTHINE DEHYDROGENASE
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence A:  ADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLG
CGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLHH
VAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVM
SMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRT
FAKSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLR
FEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEM
KFKNQLFPMIICPAWIPELNAVEHGPEGISFGAACALSSV
EKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASL
GGNIITASPISDLNPVFMASGTKLTIVSRGTRRTVPMDHT
FFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRRE
DDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALK
TTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGGMIEFR
RTLTLSFFFKFYLTVLKKLGKDSKLDPTYTSATLLFQKHP
PANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYC
DDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVC
FLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAVVAD
TPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELK
IEKGDLKKGFSEADNVVSGELYIGGQDHFYLETHCTIAIP
KGEEGEMELFVSTQNAMKTQSFVAKMLGVPVNRILVRVKR
MGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDM
LITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDL
SHSIMERALFHMDNCYKIPNIRGTGRLCKTNLSSNTAFRG
FGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLT
HFNQRLEGFSVPRCWDECLKSSQYYARKSEVDKFNKENCW
KKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSH
GGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPN
SSPTAASVSTDIYGQAVYEACQTILKRLEPFKKKNPDGSW
EDWVMAAYQDRVSLSTTGFYRTPNLGYSFETNSGNAFHYF
TYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIG
QVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFG
SIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFA
IKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKF
TTLCVTGAPGNCKPWSLRV
Description


Functional site

1) chain A
residue 867
type
sequence A
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

2) chain A
residue 870
type
sequence S
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

3) chain A
residue 871
type
sequence R
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

4) chain A
residue 874
type
sequence S
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

5) chain A
residue 907
type
sequence S
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

6) chain A
residue 908
type
sequence N
description BINDING SITE FOR RESIDUE CA A 4009
source : AC1

7) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

8) chain A
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

9) chain A
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

10) chain A
residue 116
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

11) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

12) chain A
residue 149
type
sequence R
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

13) chain A
residue 150
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3001
source : AC3

14) chain A
residue 42
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

15) chain A
residue 43
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

16) chain A
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

17) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

18) chain A
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

19) chain A
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

20) chain A
residue 49
type
sequence G
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

21) chain A
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

22) chain A
residue 71
type
sequence N
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

23) chain A
residue 73
type
sequence C
description BINDING SITE FOR RESIDUE FES A 3002
source : AC4

24) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

25) chain A
residue 150
type
sequence C
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

26) chain A
residue 796
type
sequence G
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

27) chain A
residue 797
type
sequence G
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

28) chain A
residue 798
type
sequence F
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

29) chain A
residue 912
type
sequence R
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

30) chain A
residue 1038
type
sequence M
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

31) chain A
residue 1039
type
sequence G
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

32) chain A
residue 1040
type
sequence Q
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

33) chain A
residue 1078
type
sequence A
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

34) chain A
residue 1079
type
sequence A
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

35) chain A
residue 1080
type
sequence S
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

36) chain A
residue 1081
type
sequence V
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

37) chain A
residue 1082
type
sequence S
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

38) chain A
residue 1194
type
sequence Q
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

39) chain A
residue 1261
type
sequence E
description BINDING SITE FOR RESIDUE MTE A 3003
source : AC5

40) chain A
residue 767
type
sequence Q
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

41) chain A
residue 799
type
sequence G
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

42) chain A
residue 802
type
sequence E
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

43) chain A
residue 911
type
sequence F
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

44) chain A
residue 912
type
sequence R
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

45) chain A
residue 1078
type
sequence A
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

46) chain A
residue 1079
type
sequence A
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

47) chain A
residue 1261
type
sequence E
description BINDING SITE FOR RESIDUE MOS A 3004
source : AC6

48) chain A
residue 802
type
sequence E
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

49) chain A
residue 880
type
sequence R
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

50) chain A
residue 914
type
sequence F
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

51) chain A
residue 1009
type
sequence F
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

52) chain A
residue 1010
type
sequence T
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

53) chain A
residue 1011
type
sequence V
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

54) chain A
residue 1079
type
sequence A
description BINDING SITE FOR RESIDUE SAL A 3005
source : AC7

55) chain A
residue 45
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

56) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

57) chain A
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

58) chain A
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

59) chain A
residue 256
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

60) chain A
residue 257
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

61) chain A
residue 258
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

62) chain A
residue 259
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

63) chain A
residue 260
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

64) chain A
residue 261
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

65) chain A
residue 262
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

66) chain A
residue 263
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

67) chain A
residue 264
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

68) chain A
residue 301
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

69) chain A
residue 337
type
sequence F
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

70) chain A
residue 338
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

71) chain A
residue 342
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

72) chain A
residue 346
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

73) chain A
residue 347
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

74) chain A
residue 350
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

75) chain A
residue 351
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

76) chain A
residue 353
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

77) chain A
residue 354
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

78) chain A
residue 359
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

79) chain A
residue 360
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

80) chain A
residue 403
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

81) chain A
residue 404
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

82) chain A
residue 422
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

83) chain A
residue 429
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 3006
source : AC8

84) chain A
residue 839
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

85) chain A
residue 840
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

86) chain A
residue 877
type
sequence I
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

87) chain A
residue 909
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

88) chain A
residue 910
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

89) chain A
residue 911
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

90) chain A
residue 913
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

91) chain A
residue 914
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

92) chain A
residue 915
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

93) chain A
residue 918
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 3007
source : BC6

94) chain A
residue 561
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 3008
source : BC7

95) chain A
residue 574
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 3008
source : BC7

96) chain A
residue 1184
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 3008
source : BC7

97) chain A
residue 1185
type
sequence S
description BINDING SITE FOR RESIDUE GOL A 3008
source : BC7

98) chain A
residue 802
type catalytic
sequence E
description 139
source MCSA : MCSA1

99) chain A
residue 880
type catalytic
sequence R
description 139
source MCSA : MCSA1

100) chain A
residue 1261
type catalytic
sequence E
description 139
source MCSA : MCSA1

101) 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

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

103) chain A
residue 1261
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI1

104) chain A
residue 43
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

105) chain A
residue 798
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

106) chain A
residue 912
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

107) chain A
residue 1079
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

108) chain A
residue 48
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

109) chain A
residue 51
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

110) chain A
residue 73
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

111) chain A
residue 113
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

112) chain A
residue 116
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

113) chain A
residue 148
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

114) chain A
residue 150
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

115) chain A
residue 767
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
source Swiss-Prot : SWS_FT_FI2

116) chain A
residue 257
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

117) chain A
residue 337
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

118) chain A
residue 347
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

119) chain A
residue 360
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

120) chain A
residue 404
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

121) chain A
residue 422
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
source Swiss-Prot : SWS_FT_FI3

122) chain A
residue 802
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI4

123) chain A
residue 880
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI4

124) chain A
residue 914
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI4

125) chain A
residue 1010
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI4


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