eF-site ID 6q9d-.A2.A5.A6.A7.A9.AA.AL.AM.S1.S2.S3.S4.S6.S7.S8.V1.V2.V3
PDB Code 6q9d
Chain A2, A5, A6, A7, A9, AA, AL, AM, S1, S2, S3, S4, S6, S7, S8, V1, V2, V3
Title CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2
Classification ELECTRON TRANSPORT
Compound NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
Source ORGANISM_COMMON: Sheep; ORGANISM_SCIENTIFIC: Ovis aries;
Sequence A2:  LGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPI
LIRECSDVQPKLWARYAFGQEKNVSLNNFSADQVTRALEN
VL
A5:  KKTTGLVGLAVCETPHERLKILYTKILDVLGHIPKNAAYR
KYTEQITNEKLSIVKAEPDVKKLEEQLQGGQIEEVILQAE
NELSLARKMIQWKPWEPLVEEPPASQWKWPI
A6:  TSVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHLFQLDI
SVKQGRDKVREMFKKNAHVTDPRVVDLLVIKGKMELEETI
NVWKQRTHVMRFFHETEAPRPKDFLSKFYVGHDP
A7:  ASATRLIQGLRNWASGRDLQAKLQLRYQEISKRTQPPPKL
PVGPSHRLSNNYYCARDGRREAMPPSIVMSSQSEKKAVSP
APPIKRWELSQDEPYL
A9:  LHHAVIPHGKGGRSSVSGIVATVFGATGFLGRYLVNHLGR
MGSQVIVPYRCEPYDTMHLRPMGDLGQIIFMDWNGRDKDS
IRRAVEHSNVVINLVGREWETKNFDFEDVFVKIPQAIAQV
SKEAGVEKFIHISHLNADIKSSSKYLRNKAVGEKEVRETF
PEATIIKPADIFGREDRFLNYFANIRSLGKKTVKQPVYIV
DVTKGIINAIKDPDARGKTFAFVGPNRYLLFDLVQYVFAV
AHRPFLWTTRDKVERIHTTDRTLPHLPGLEDLGVQATPLE
LKAIEVLRRHRTYRSEIEDVQPA
AA:  PLTLEGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDS
LDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKK
AL:  LKRGLQQVSGHGGLRGYLRVLFRANDVRVGTLVGEDKYGN
KYYEDNKQFFGRHRWVIYTTEMNGKNTFWDVDGSMVPPEW
HRWLHCMTDDPPTVKPPTARKFIWTNHKFNLSGTPQQYVP
YSTTRKKIQEWVPPSTPYK
AM:  VKQDMPPVGGYGPIDYKRNLPRR
S1:  SNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHER
LSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEK
TKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGS
DRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASE
IAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPV
GALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTG
EVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVR
NEKGLLTHTTWEDALSRVAGMLQSCQGNDVAAIAGGLVDA
EALIALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLN
TTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLK
VALIGSPVDLTYRYDHLGDSPKILQDIASGSHPFSQVLQE
AKKPMVVLGSSALQRNDGAAILAAVSNIAQKIRTSSGVTG
DWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKMLFLL
GADGGCVTRQDLPKDCFIVYQGHHGDVGAPIADVILPGAA
YTEKSATYVNTEGRAQQTKVAVMPPGLAREDWKIIRALSE
IAGMTLPYDTLDQVRNRLEEVSPNLVRYDDVEGANYFQQA
SELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMA
KCVKAVTE
S2:  SNLTLNFGPQHPGVLRLVMELSGEMVRKCDPHIGLLHRGT
EKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLN
IQPPPRAQWIRVLFGEITRLLNHIMAVTTHALDIGAMTPF
FWMFEEREKMFEFYERVSGARMHAAYVRPGGVHQDLPLGL
MDDIYEFSKNFSLRIDELEEMLTNNRIWRNRTVDIGVVTA
EDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPI
GSRGDCYDRYLCRVEEMRQSIRIISQCLNKMPPGEIKVDD
AKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAI
EAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSK
GHMLADVVAIIGTQDIVFGEVDR
S3:  TRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFS
ELEICIHPDGVIPVLTFLRDHSNAQFKSLADLTAVDIPTR
QNRFEIVYNLLSLRFNSRIRVKTYTDELTPVESSVSVYKA
ANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDF
PLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAF
PAYRQPPE
S4:  TQLITVDEKLDITTLTGVPEEHIKTRKARIFVPARNNMQS
GVNNTKKWKMEFDTRERWENPLMGWASTADPLSNLVLTFS
TKEDAIAFAEKNGWSYDVEERKVPKPKSKSYGANFSWNKR
TRVSTK
S6:  GVRTSPTGEKVTHTGQVYDDEDYRRVRFVGRQKEVNENFA
IDLIAEQPVSQVGSRVISCDGGGGALGHPRVYINLDKETK
TGTCGYCGLQFRQQH
S7:  SRGEYVVAKLDDLINWARRSSLWPMTFGLACCAVEMMHMA
APRYDMDRFGVVFRASPRQSDVMIVAGTLTNKMAPALRKV
YDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVD
IYVPGCPPTAEALLYGILQLQKKIKREKRLRIWYRR
S8:  TYKYVNLREPSMDMKSVTDRAAQTLLWTELIRGLGMTLSY
LFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIAC
KLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCG
FCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDK
WEAEIAANIQADYLYR
V1:  KTSFGSLKDEDRIFTNLYGRHDWRLKGAQSRGDWYKTKEI
LLKGPDWILGEVKTSGLRGRGGAGFPTGLKWSFMNKPSDG
RPKYLVVNADEGEPGTCKDREIIRHDPHKLVEGCLVGGRA
MGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACG
SGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPP
FPADVGVFGCPTTVANVETVAVSPTICRRGGAWFASFGRE
RNSGTKLFNISGHVNNPCTVEEEMSVPLKELIEKHAGGVT
GGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALIQAQTG
LGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREG
VDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALG
DGAAWPVQGLIRHFRPELEERMQRFAQQHQ
V2:  ALFVHRDTPKNNPETPFDFTPENYKRIEAIVKNYPEGHKA
AAVLPVLDLAQRQNGWLPISAMNKVAEILQVPPMRVYEVA
TFYTMYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKL
GIKVGETTPDKLFTLIEVECLGACVNAPMVQINDNYYEDL
TPKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTE
PPKGPGFGVQAG
V3:  NTTYKNLQHHDYSTYTFLDLNLDLSKFRMPQPSSGRESPR
H
Description (1)  NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (E.C.1.6.99.3,7.1.1.2), NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH:ubiquinone oxidoreductase core subunit S1, NADH:ubiquinone oxidoreductase core subunit S2,NADH:ubiquinone oxidoreductase core subunit S2, NADH:ubiquinone oxidoreductase core subunit S3, NADH:ubiquinone oxidoreductase core subunit S7, NADH:ubiquinone oxidoreductase core subunit S8, NADH:ubiquinone oxidoreductase subunit V3, NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial, NADH:ubiquinone oxidoreductase subunit S4, NADH:ubiquinone oxidoreductase subunit A9, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, NADH:ubiquinone oxidoreductase subunit A6, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12, Acyl carrier protein, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13


Functional site

1) chain V1
residue 203
type
sequence P
description binding site for residue SF4 V1 500
source : AC1

2) chain V1
residue 358
type
sequence S
description binding site for residue SF4 V1 500
source : AC1

3) chain V1
residue 359
type
sequence C
description binding site for residue SF4 V1 500
source : AC1

4) chain V1
residue 360
type
sequence G
description binding site for residue SF4 V1 500
source : AC1

5) chain V1
residue 361
type
sequence Q
description binding site for residue SF4 V1 500
source : AC1

6) chain V1
residue 362
type
sequence C
description binding site for residue SF4 V1 500
source : AC1

7) chain V1
residue 365
type
sequence C
description binding site for residue SF4 V1 500
source : AC1

8) chain V1
residue 403
type
sequence T
description binding site for residue SF4 V1 500
source : AC1

9) chain V1
residue 404
type
sequence I
description binding site for residue SF4 V1 500
source : AC1

10) chain V1
residue 405
type
sequence C
description binding site for residue SF4 V1 500
source : AC1

11) chain V1
residue 67
type
sequence G
description binding site for residue FMN V1 501
source : AC2

12) chain V1
residue 68
type
sequence R
description binding site for residue FMN V1 501
source : AC2

13) chain V1
residue 69
type
sequence G
description binding site for residue FMN V1 501
source : AC2

14) chain V1
residue 71
type
sequence A
description binding site for residue FMN V1 501
source : AC2

15) chain V1
residue 73
type
sequence F
description binding site for residue FMN V1 501
source : AC2

16) chain V1
residue 78
type
sequence K
description binding site for residue FMN V1 501
source : AC2

17) chain V1
residue 96
type
sequence N
description binding site for residue FMN V1 501
source : AC2

18) chain V1
residue 98
type
sequence D
description binding site for residue FMN V1 501
source : AC2

19) chain V1
residue 184
type
sequence Y
description binding site for residue FMN V1 501
source : AC2

20) chain V1
residue 187
type
sequence G
description binding site for residue FMN V1 501
source : AC2

21) chain V1
residue 188
type
sequence E
description binding site for residue FMN V1 501
source : AC2

22) chain V1
residue 222
type
sequence V
description binding site for residue FMN V1 501
source : AC2

23) chain V1
residue 224
type
sequence N
description binding site for residue FMN V1 501
source : AC2

24) chain V1
residue 227
type
sequence T
description binding site for residue FMN V1 501
source : AC2

25) chain V2
residue 103
type
sequence C
description binding site for residue FES V2 300
source : AC3

26) chain V2
residue 105
type
sequence T
description binding site for residue FES V2 300
source : AC3

27) chain V2
residue 108
type
sequence C
description binding site for residue FES V2 300
source : AC3

28) chain V2
residue 144
type
sequence C
description binding site for residue FES V2 300
source : AC3

29) chain V2
residue 145
type
sequence L
description binding site for residue FES V2 300
source : AC3

30) chain V2
residue 146
type
sequence G
description binding site for residue FES V2 300
source : AC3

31) chain V2
residue 147
type
sequence A
description binding site for residue FES V2 300
source : AC3

32) chain V2
residue 148
type
sequence C
description binding site for residue FES V2 300
source : AC3

33) chain S1
residue 101
type
sequence H
description binding site for residue SF4 S1 801
source : AC4

34) chain S1
residue 104
type
sequence D
description binding site for residue SF4 S1 801
source : AC4

35) chain S1
residue 105
type
sequence C
description binding site for residue SF4 S1 801
source : AC4

36) chain S1
residue 108
type
sequence C
description binding site for residue SF4 S1 801
source : AC4

37) chain S1
residue 114
type
sequence C
description binding site for residue SF4 S1 801
source : AC4

38) chain S1
residue 117
type
sequence Q
description binding site for residue SF4 S1 801
source : AC4

39) chain S1
residue 205
type
sequence V
description binding site for residue SF4 S1 801
source : AC4

40) chain S1
residue 206
type
sequence G
description binding site for residue SF4 S1 801
source : AC4

41) chain S1
residue 153
type
sequence C
description binding site for residue SF4 S1 802
source : AC5

42) chain S1
residue 154
type
sequence I
description binding site for residue SF4 S1 802
source : AC5

43) chain S1
residue 156
type
sequence C
description binding site for residue SF4 S1 802
source : AC5

44) chain S1
residue 157
type
sequence T
description binding site for residue SF4 S1 802
source : AC5

45) chain S1
residue 159
type
sequence C
description binding site for residue SF4 S1 802
source : AC5

46) chain S1
residue 203
type
sequence C
description binding site for residue SF4 S1 802
source : AC5

47) chain S1
residue 205
type
sequence V
description binding site for residue SF4 S1 802
source : AC5

48) chain S1
residue 41
type
sequence C
description binding site for residue FES S1 803
source : AC6

49) chain S1
residue 42
type
sequence Y
description binding site for residue FES S1 803
source : AC6

50) chain S1
residue 50
type
sequence G
description binding site for residue FES S1 803
source : AC6

51) chain S1
residue 52
type
sequence C
description binding site for residue FES S1 803
source : AC6

52) chain S1
residue 53
type
sequence R
description binding site for residue FES S1 803
source : AC6

53) chain S1
residue 55
type
sequence C
description binding site for residue FES S1 803
source : AC6

54) chain S1
residue 69
type
sequence C
description binding site for residue FES S1 803
source : AC6

55) chain S2
residue 105
type
sequence R
description binding site for residue SF4 S7 300
source : AC7

56) chain S7
residue 53
type
sequence A
description binding site for residue SF4 S7 300
source : AC7

57) chain S7
residue 54
type
sequence C
description binding site for residue SF4 S7 300
source : AC7

58) chain S7
residue 55
type
sequence C
description binding site for residue SF4 S7 300
source : AC7

59) chain S7
residue 90
type
sequence G
description binding site for residue SF4 S7 300
source : AC7

60) chain S7
residue 117
type
sequence G
description binding site for residue SF4 S7 300
source : AC7

61) chain S7
residue 118
type
sequence S
description binding site for residue SF4 S7 300
source : AC7

62) chain S7
residue 119
type
sequence C
description binding site for residue SF4 S7 300
source : AC7

63) chain S7
residue 149
type
sequence C
description binding site for residue SF4 S7 300
source : AC7

64) chain S7
residue 150
type
sequence P
description binding site for residue SF4 S7 300
source : AC7

65) chain S8
residue 87
type
sequence C
description binding site for residue SF4 S8 201
source : AC8

66) chain S8
residue 88
type
sequence P
description binding site for residue SF4 S8 201
source : AC8

67) chain S8
residue 92
type
sequence I
description binding site for residue SF4 S8 201
source : AC8

68) chain S8
residue 116
type
sequence C
description binding site for residue SF4 S8 201
source : AC8

69) chain S8
residue 117
type
sequence I
description binding site for residue SF4 S8 201
source : AC8

70) chain S8
residue 118
type
sequence Y
description binding site for residue SF4 S8 201
source : AC8

71) chain S8
residue 119
type
sequence C
description binding site for residue SF4 S8 201
source : AC8

72) chain S8
residue 120
type
sequence G
description binding site for residue SF4 S8 201
source : AC8

73) chain S8
residue 122
type
sequence C
description binding site for residue SF4 S8 201
source : AC8

74) chain S8
residue 133
type
sequence E
description binding site for residue SF4 S8 201
source : AC8

75) chain S8
residue 77
type
sequence C
description binding site for residue SF4 S8 202
source : AC9

76) chain S8
residue 78
type
sequence I
description binding site for residue SF4 S8 202
source : AC9

77) chain S8
residue 79
type
sequence A
description binding site for residue SF4 S8 202
source : AC9

78) chain S8
residue 80
type
sequence C
description binding site for residue SF4 S8 202
source : AC9

79) chain S8
residue 81
type
sequence K
description binding site for residue SF4 S8 202
source : AC9

80) chain S8
residue 83
type
sequence C
description binding site for residue SF4 S8 202
source : AC9

81) chain S8
residue 126
type
sequence C
description binding site for residue SF4 S8 202
source : AC9

82) chain S8
residue 131
type
sequence I
description binding site for residue SF4 S8 202
source : AC9

83) chain S6
residue 59
type
sequence C
description binding site for residue ZN S6 300
source : AD1

84) chain S6
residue 68
type
sequence H
description binding site for residue ZN S6 300
source : AD1

85) chain S6
residue 71
type
sequence V
description binding site for residue ZN S6 300
source : AD1

86) chain S6
residue 84
type
sequence C
description binding site for residue ZN S6 300
source : AD1

87) chain S6
residue 87
type
sequence C
description binding site for residue ZN S6 300
source : AD1

88) chain A9
residue 27
type
sequence T
description binding site for residue NDP A9 401
source : AD2

89) chain A9
residue 28
type
sequence G
description binding site for residue NDP A9 401
source : AD2

90) chain A9
residue 29
type
sequence F
description binding site for residue NDP A9 401
source : AD2

91) chain A9
residue 30
type
sequence L
description binding site for residue NDP A9 401
source : AD2

92) chain A9
residue 50
type
sequence R
description binding site for residue NDP A9 401
source : AD2

93) chain A9
residue 95
type
sequence V
description binding site for residue NDP A9 401
source : AD2

94) chain A9
residue 96
type
sequence G
description binding site for residue NDP A9 401
source : AD2

95) chain A9
residue 97
type
sequence R
description binding site for residue NDP A9 401
source : AD2

96) chain A9
residue 132
type
sequence I
description binding site for residue NDP A9 401
source : AD2

97) chain A9
residue 134
type
sequence H
description binding site for residue NDP A9 401
source : AD2

98) chain A9
residue 145
type
sequence Y
description binding site for residue NDP A9 401
source : AD2

99) chain A9
residue 149
type
sequence K
description binding site for residue NDP A9 401
source : AD2

100) chain A9
residue 169
type
sequence A
description binding site for residue NDP A9 401
source : AD2

101) chain A9
residue 171
type
sequence I
description binding site for residue NDP A9 401
source : AD2

102) chain A9
residue 177
type
sequence R
description binding site for residue NDP A9 401
source : AD2

103) chain A6
residue 28
type
sequence K
description binding site for residue ZMP AA 101
source : AD3

104) chain A6
residue 32
type
sequence R
description binding site for residue ZMP AA 101
source : AD3

105) chain A6
residue 38
type
sequence W
description binding site for residue ZMP AA 101
source : AD3

106) chain A6
residue 62
type
sequence V
description binding site for residue ZMP AA 101
source : AD3

107) chain A6
residue 66
type
sequence F
description binding site for residue ZMP AA 101
source : AD3

108) chain A6
residue 69
type
sequence N
description binding site for residue ZMP AA 101
source : AD3

109) chain A6
residue 70
type
sequence A
description binding site for residue ZMP AA 101
source : AD3

110) chain A6
residue 81
type
sequence L
description binding site for residue ZMP AA 101
source : AD3

111) chain AA
residue 43
type
sequence D
description binding site for residue ZMP AA 101
source : AD3

112) chain AA
residue 44
type
sequence S
description binding site for residue ZMP AA 101
source : AD3

113) chain S8
residue 77-88
type prosite
sequence CIACKLCEAVCP
description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
source prosite : PS00198

114) chain S8
residue 116-127
type prosite
sequence CIYCGFCQEACP
description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
source prosite : PS00198

115) chain V1
residue 180-195
type prosite
sequence GAGAYICGEETALIES
description COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
source prosite : PS00644

116) chain S1
residue 105-117
type prosite
sequence CPICDQGGECDLQ
description COMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
source prosite : PS00642

117) chain S1
residue 152-162
type prosite
sequence RCIQCTRCIRF
description COMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
source prosite : PS00643

118) chain V2
residue 134-152
type prosite
sequence DKLFTLIEVECLGACVNAP
description COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
source prosite : PS01099

119) chain S1
residue 38-55
type prosite
sequence PRFCYHERLSVAGNCRMC
description COMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
source prosite : PS00641

120) chain V1
residue 357-368
type prosite
sequence ESCGQCTPCREG
description COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
source prosite : PS00645

121) chain AA
residue 39-54
type prosite
sequence DLGLDSLDQVEIIMAM
description PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
source prosite : PS00012

122) chain AA
residue 64-76
type prosite
sequence DIDAEKLMCPQEI
description EF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
source prosite : PS00018

123) chain S2
residue 83-94
type prosite
sequence LHRGTEKLIEYK
description COMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
source prosite : PS00535

124) chain S3
residue 131-152
type prosite
sequence EREIWDMFGVFFANHPDLRRIL
description COMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
source prosite : PS00542

125) chain S7
residue 135-151
type prosite
sequence GCDRIVPVDIYVPGCPP
description COMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
source prosite : PS01150


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