eF-site ID 5fcr-ABCD
PDB Code 5fcr
Chain A, B, C, D

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Title MOUSE COMPLEMENT FACTOR D
Classification HYDROLASE
Compound Complement factor D
Source Mus musculus (Mouse) (CFAD_MOUSE)
Sequence A:  ILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAA
HCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHP
GSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEP
GTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTY
HDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTW
GSRVCGNGKKPGVYTRVSSYRMWIENITNG
B:  ILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAA
HCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHP
GSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEP
GTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTY
HDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTW
GSRVCGNGKKPGVYTRVSSYRMWIENITNG
C:  ILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAA
HCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHP
GSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEP
GTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTY
HDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTW
GSRVCGNGKKPGVYTRVSSYRMWIENITN
D:  ILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAA
HCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHP
GSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEP
GTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTY
HDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTW
GSRVCGNGKKPGVYTRVSSYRMWIENITNG
Description


Functional site

1) chain B
residue 91
type
sequence H
description binding site for residue EPE B 301
source : AC1

2) chain B
residue 100
type
sequence E
description binding site for residue EPE B 301
source : AC1

3) chain B
residue 101
type
sequence D
description binding site for residue EPE B 301
source : AC1

4) chain B
residue 179
type
sequence N
description binding site for residue EPE B 301
source : AC1

5) chain B
residue 233
type
sequence S
description binding site for residue EPE B 301
source : AC1

6) chain B
residue 234
type
sequence Y
description binding site for residue EPE B 301
source : AC1

7) chain B
residue 236
type
sequence M
description binding site for residue EPE B 301
source : AC1

8) chain B
residue 237
type
sequence W
description binding site for residue EPE B 301
source : AC1

9) chain B
residue 21
type
sequence E
description binding site for residue GOL B 302
source : AC2

10) chain B
residue 150
type
sequence R
description binding site for residue GOL B 302
source : AC2

11) chain B
residue 152
type
sequence P
description binding site for residue GOL B 302
source : AC2

12) chain B
residue 153
type
sequence D
description binding site for residue GOL B 302
source : AC2

13) chain B
residue 154
type
sequence V
description binding site for residue GOL B 302
source : AC2

14) chain B
residue 156
type
sequence H
description binding site for residue GOL B 302
source : AC2

15) chain C
residue 91
type
sequence H
description binding site for residue EPE C 301
source : AC3

16) chain C
residue 100
type
sequence E
description binding site for residue EPE C 301
source : AC3

17) chain C
residue 101
type
sequence D
description binding site for residue EPE C 301
source : AC3

18) chain C
residue 179
type
sequence N
description binding site for residue EPE C 301
source : AC3

19) chain C
residue 233
type
sequence S
description binding site for residue EPE C 301
source : AC3

20) chain C
residue 234
type
sequence Y
description binding site for residue EPE C 301
source : AC3

21) chain C
residue 236
type
sequence M
description binding site for residue EPE C 301
source : AC3

22) chain C
residue 237
type
sequence W
description binding site for residue EPE C 301
source : AC3

23) chain C
residue 150
type
sequence R
description binding site for residue SO4 C 302
source : AC4

24) chain C
residue 152
type
sequence P
description binding site for residue SO4 C 302
source : AC4

25) chain C
residue 153
type
sequence D
description binding site for residue SO4 C 302
source : AC4

26) chain C
residue 154
type
sequence V
description binding site for residue SO4 C 302
source : AC4

27) chain C
residue 156
type
sequence H
description binding site for residue SO4 C 302
source : AC4

28) chain D
residue 91
type
sequence H
description binding site for residue DMS D 301
source : AC5

29) chain D
residue 234
type
sequence Y
description binding site for residue DMS D 301
source : AC5

30) chain D
residue 236
type
sequence M
description binding site for residue DMS D 301
source : AC5

31) chain D
residue 237
type
sequence W
description binding site for residue DMS D 301
source : AC5

32) chain D
residue 21
type
sequence E
description binding site for residue DMS D 302
source : AC6

33) chain D
residue 150
type
sequence R
description binding site for residue DMS D 302
source : AC6

34) chain D
residue 152
type
sequence P
description binding site for residue DMS D 302
source : AC6

35) chain D
residue 153
type
sequence D
description binding site for residue DMS D 302
source : AC6

36) chain D
residue 154
type
sequence V
description binding site for residue DMS D 302
source : AC6

37) chain D
residue 156
type
sequence H
description binding site for residue DMS D 302
source : AC6

38) chain A
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

39) chain D
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

40) chain D
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

41) chain D
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

45) chain B
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

47) chain C
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

48) chain C
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

49) chain C
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 53-58
type prosite
sequence LSAAHC
description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC
source prosite : PS00134

51) chain A
residue 189-200
type prosite
sequence DTCRGDSGSPLV
description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DTcrGDSGSPLV
source prosite : PS00135

52) chain A
residue 111
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957
source Swiss-Prot : SWS_FT_FI3

53) chain B
residue 111
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957
source Swiss-Prot : SWS_FT_FI3

54) chain C
residue 111
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957
source Swiss-Prot : SWS_FT_FI3

55) chain D
residue 111
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957
source Swiss-Prot : SWS_FT_FI3

56) chain A
residue 164
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
source Swiss-Prot : SWS_FT_FI4

57) chain B
residue 164
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
source Swiss-Prot : SWS_FT_FI4

58) chain C
residue 164
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
source Swiss-Prot : SWS_FT_FI4

59) chain D
residue 164
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
source Swiss-Prot : SWS_FT_FI4

60) chain A
residue 36
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

61) chain D
residue 36
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

62) chain D
residue 240
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

63) chain A
residue 240
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

64) chain B
residue 36
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

65) chain B
residue 240
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

66) chain C
residue 36
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

67) chain C
residue 240
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI2


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