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

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Title STRUCTURE OF DICERIC HUMAN LACTOFERRIN
Classification METAL TRANSPORT
Compound LACTOFERRIN
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  RRRRSVQWCAVSNPEATKCFQWQRNMRKVRGPPVSCIKRD
SPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAE
VYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLR
RTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPG
ADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLR
DGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVD
KFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGK
DKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYL
GSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQ
WSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVY
TAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAV
VRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQT
GSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPN
SNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNE
AWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVV
SRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKN
LLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTS
PLLEACEFLRK
Description (1)  LACTOFERRIN


Functional site

1) chain A
residue 60
type
sequence D
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

2) chain A
residue 92
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

3) chain A
residue 117
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

4) chain A
residue 121
type
sequence R
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

5) chain A
residue 122
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

6) chain A
residue 123
type
sequence A
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

7) chain A
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

8) chain A
residue 192
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 695
source : AC1

9) chain A
residue 395
type
sequence D
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

10) chain A
residue 461
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

11) chain A
residue 465
type
sequence R
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

12) chain A
residue 466
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

13) chain A
residue 467
type
sequence A
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

14) chain A
residue 468
type
sequence G
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

15) chain A
residue 528
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 696
source : AC2

16) chain A
residue 60
type
sequence D
description BINDING SITE FOR RESIDUE CE A 693
source : AC3

17) chain A
residue 92
type
sequence Y
description BINDING SITE FOR RESIDUE CE A 693
source : AC3

18) chain A
residue 192
type
sequence Y
description BINDING SITE FOR RESIDUE CE A 693
source : AC3

19) chain A
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE CE A 693
source : AC3

20) chain A
residue 395
type
sequence D
description BINDING SITE FOR RESIDUE CE A 694
source : AC4

21) chain A
residue 435
type
sequence Y
description BINDING SITE FOR RESIDUE CE A 694
source : AC4

22) chain A
residue 528
type
sequence Y
description BINDING SITE FOR RESIDUE CE A 694
source : AC4

23) chain A
residue 597
type
sequence H
description BINDING SITE FOR RESIDUE CE A 694
source : AC4

24) chain A
residue 92-101
type prosite
sequence YYAVAVVKKG
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
source prosite : PS00205

25) chain A
residue 435-444
type prosite
sequence YLAVAVVRRS
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
source prosite : PS00205

26) chain A
residue 192-208
type prosite
sequence YSGAFKCLRDGAGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
source prosite : PS00206

27) chain A
residue 528-544
type prosite
sequence YTGAFRCLAENAGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
source prosite : PS00206

28) chain A
residue 226-256
type prosite
sequence EYELLCPDNTRKPVDKFKDCHLARVPSHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
source prosite : PS00207

29) chain A
residue 570-600
type prosite
sequence DFALLCLDGKRKPVTEARSCHLAMAPNHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
source prosite : PS00207

30) chain A
residue 73
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000305|PubMed:12535064
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 259
type ACT_SITE
sequence S
description Nucleophile => ECO:0000305|PubMed:12535064
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 60
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 92
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 192
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 253
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 395
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 435
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 528
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 597
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 117
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

41) chain A
residue 121
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

42) chain A
residue 123
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 124
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

44) chain A
residue 461
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

45) chain A
residue 465
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

46) chain A
residue 467
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

47) chain A
residue 468
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI4

48) chain A
residue 4
type SITE
sequence R
description Interaction with PspA
source Swiss-Prot : SWS_FT_FI5

49) chain A
residue 13
type SITE
sequence N
description Interaction with PspA
source Swiss-Prot : SWS_FT_FI5

50) chain A
residue 210
type SITE
sequence R
description Important for iron binding
source Swiss-Prot : SWS_FT_FI6

51) chain A
residue 137
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8069634, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI7

52) chain A
residue 478
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.72
source Swiss-Prot : SWS_FT_FI8

53) chain A
residue 623
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
source Swiss-Prot : SWS_FT_FI9


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