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

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Title STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN
Classification IRON-BINDING PROTEIN
Compound LACTOFERRIN
Source ORGANISM_COMMON: water buffalo; ORGANISM_SCIENTIFIC: Bubalus bubalis;
Sequence A:  APRKNVRWCTISQPEWLKCHRWQWRMKKLGAPSITCVRRA
FVLECIRAITEKKADAVTLDGGMVFEAGLDPYKLRPVAAE
IYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRNSCHTGLG
RSAGWNIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPC
VDRQAYPNLCQLCKGEGENQCACSPREPYFGYSGAFKCLQ
DGAGDVAFVKETTVFENLPEKADRDQYELLCLNNTRAPVD
AFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGK
NKSGSFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYL
GSRYLTALKNLRETAEEVQARRARVVWCAVGPEEQKKCQQ
WSQQSGQIVTCATASTTDDCIALVLKGEADALSLDGGYIY
TAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVK
KANEGLTWNSLKGKKSCHTAVDRTAGWNIPMGLIANQTGS
CAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSK
EKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADW
AKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSL
SERAAHVEQVLLHQQALFGENGKNCPDKFCLFKSETKNLL
FNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPL
LEACAFLTR
Description


Functional site
1) chain A
residue 60
type
sequence D
description IRON BINDING SITE IN N-LOBE.
source : FE1
2) chain A
residue 92
type
sequence Y
description IRON BINDING SITE IN N-LOBE.
source : FE1
3) chain A
residue 192
type
sequence Y
description IRON BINDING SITE IN N-LOBE.
source : FE1
4) chain A
residue 253
type
sequence H
description IRON BINDING SITE IN N-LOBE.
source : FE1
5) chain A
residue 395
type
sequence D
description IRON BINDING SITE IN C-LOBE.
source : FE2
6) chain A
residue 433
type
sequence Y
description IRON BINDING SITE IN C-LOBE.
source : FE2
7) chain A
residue 526
type
sequence Y
description IRON BINDING SITE IN C-LOBE.
source : FE2
8) chain A
residue 595
type
sequence H
description IRON BINDING SITE IN C-LOBE.
source : FE2
9) chain A
residue 60
type
sequence D
description BINDING SITE FOR RESIDUE FE A 690
source : AC1
10) chain A
residue 92
type
sequence Y
description BINDING SITE FOR RESIDUE FE A 690
source : AC1
11) chain A
residue 192
type
sequence Y
description BINDING SITE FOR RESIDUE FE A 690
source : AC1
12) chain A
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE FE A 690
source : AC1
13) chain A
residue 395
type
sequence D
description BINDING SITE FOR RESIDUE FE A 691
source : AC2
14) chain A
residue 433
type
sequence Y
description BINDING SITE FOR RESIDUE FE A 691
source : AC2
15) chain A
residue 526
type
sequence Y
description BINDING SITE FOR RESIDUE FE A 691
source : AC2
16) chain A
residue 595
type
sequence H
description BINDING SITE FOR RESIDUE FE A 691
source : AC2
17) chain A
residue 60
type
sequence D
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
18) chain A
residue 92
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
19) chain A
residue 117
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
20) chain A
residue 121
type
sequence R
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
21) chain A
residue 123
type
sequence A
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
22) chain A
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
23) chain A
residue 192
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
24) chain A
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE CO3 A 692
source : AC3
25) chain A
residue 395
type
sequence D
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
26) chain A
residue 433
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
27) chain A
residue 459
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
28) chain A
residue 463
type
sequence R
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
29) chain A
residue 464
type
sequence T
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
30) chain A
residue 465
type
sequence A
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
31) chain A
residue 466
type
sequence G
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
32) chain A
residue 526
type
sequence Y
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
33) chain A
residue 595
type
sequence H
description BINDING SITE FOR RESIDUE CO3 A 693
source : AC4
34) chain A
residue 433-442
type prosite
sequence YLAVAVVKKA
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
source prosite : PS00205
35) chain A
residue 92-101
type prosite
sequence YYAVAVVKKG
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
source prosite : PS00205
36) chain A
residue 192-208
type prosite
sequence YSGAFKCLQDGAGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF
source prosite : PS00206
37) chain A
residue 526-542
type prosite
sequence YTGAFRCLAEDVGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF
source prosite : PS00206
38) chain A
residue 226-256
type prosite
sequence QYELLCLNNTRAPVDAFKECHLAQVPSHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNntrap...VdafkeChlAqvpsHaVV
source prosite : PS00207
39) chain A
residue 568-598
type prosite
sequence DFRLLCLDGTRKPVTEAQSCHLAVAPNHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNntrap...VdafkeChlAqvpsHaVV
source prosite : PS00207
40) chain A
residue 73
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI1
41) chain A
residue 259
type ACT_SITE
sequence S
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI2
42) chain A
residue 253
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
43) chain A
residue 395
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
44) chain A
residue 433
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
45) chain A
residue 526
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
46) chain A
residue 595
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
47) chain A
residue 60
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
48) chain A
residue 92
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344, ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI3
49) chain A
residue 121
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
50) chain A
residue 123
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
51) chain A
residue 124
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
52) chain A
residue 459
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
53) chain A
residue 463
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
54) chain A
residue 465
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
55) chain A
residue 466
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
56) chain A
residue 117
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10531476, ECO:0000269|PubMed:10818344
source Swiss-Prot : SWS_FT_FI4
57) chain A
residue 192
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:1BIY, ECO:0007744|PDB:1CE2
source Swiss-Prot : SWS_FT_FI5
58) chain A
residue 545
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
source Swiss-Prot : SWS_FT_FI6
59) chain A
residue 233
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
source Swiss-Prot : SWS_FT_FI6
60) chain A
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
source Swiss-Prot : SWS_FT_FI7
61) chain A
residue 476
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.105215
source Swiss-Prot : SWS_FT_FI8

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