|
|
eF-site ID
|
1lct-A |
|
PDB Code
|
1lct |
|
Chain
|
A |
|
click to enlarge
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Title
|
STRUCTURE OF THE RECOMBINANT N-TERMINAL LOBE OF HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION |
|
Classification
|
IRON TRANSPORT |
|
Compound
|
LACTOFERRIN |
|
Source
|
Homo sapiens (Human) (TRFL_HUMAN) |
|
|
Sequence
|
A: |
RSVQWCAVSNPEATKCFQWQRNMRKVRGPPVSCIKRDSPI
QCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYG
TERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTA
GWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADK
GQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGA
GDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFK
DCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKS
PKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSG
YFTA
|
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Description
|
(1) |
LACTOFERRIN (N-TERMINAL HALF-MOLECULE)
|
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Functional site
|
|
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1)
|
chain |
A |
| residue |
60 |
| type |
|
| sequence |
D
|
| description |
|
| source |
: BST
|
|
|
2)
|
chain |
A |
| residue |
92 |
| type |
|
| sequence |
Y
|
| description |
|
| source |
: BST
|
|
|
3)
|
chain |
A |
| residue |
117 |
| type |
|
| sequence |
T
|
| description |
|
| source |
: BST
|
|
|
4)
|
chain |
A |
| residue |
121 |
| type |
|
| sequence |
R
|
| description |
|
| source |
: BST
|
|
|
5)
|
chain |
A |
| residue |
123 |
| type |
|
| sequence |
A
|
| description |
|
| source |
: BST
|
|
|
6)
|
chain |
A |
| residue |
124 |
| type |
|
| sequence |
G
|
| description |
|
| source |
: BST
|
|
|
7)
|
chain |
A |
| residue |
192 |
| type |
|
| sequence |
Y
|
| description |
|
| source |
: BST
|
|
|
8)
|
chain |
A |
| residue |
253 |
| type |
|
| sequence |
H
|
| description |
|
| source |
: BST
|
|
|
9)
|
chain |
A |
| residue |
60 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE FE A 400
|
| source |
: AC1
|
|
|
10)
|
chain |
A |
| residue |
92 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE FE A 400
|
| source |
: AC1
|
|
|
11)
|
chain |
A |
| residue |
192 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE FE A 400
|
| source |
: AC1
|
|
|
12)
|
chain |
A |
| residue |
253 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE FE A 400
|
| source |
: AC1
|
|
|
13)
|
chain |
A |
| residue |
60 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
14)
|
chain |
A |
| residue |
92 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
15)
|
chain |
A |
| residue |
117 |
| type |
|
| sequence |
T
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
16)
|
chain |
A |
| residue |
121 |
| type |
|
| sequence |
R
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
17)
|
chain |
A |
| residue |
123 |
| type |
|
| sequence |
A
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
18)
|
chain |
A |
| residue |
124 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
19)
|
chain |
A |
| residue |
192 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
20)
|
chain |
A |
| residue |
253 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE CO3 A 401
|
| source |
: AC2
|
|
|
21)
|
chain |
A |
| residue |
72 |
| type |
ACT_SITE |
| sequence |
Y
|
| description |
ACT_SITE => ECO:0000305|PubMed:12535064
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
22)
|
chain |
A |
| residue |
258 |
| type |
ACT_SITE |
| sequence |
R
|
| description |
Nucleophile => ECO:0000305|PubMed:12535064
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
23)
|
chain |
A |
| residue |
12 |
| type |
SITE |
| sequence |
S
|
| description |
Interaction with PspA
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
24)
|
chain |
A |
| residue |
209 |
| type |
SITE |
| sequence |
I
|
| description |
Important for iron binding
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
25)
|
chain |
A |
| residue |
92-101 |
| type |
prosite |
| sequence |
YYAVAVVKKG
|
| 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 |
226-256 |
| type |
prosite |
| sequence |
EYELLCPDNTRKPVDKFKDCHLARVPSHAVV
|
| description |
TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
|
| source |
prosite : PS00207
|
|
|
28)
|
chain |
A |
| residue |
59 |
| type |
BINDING |
| sequence |
L
|
| 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
|
|
|
29)
|
chain |
A |
| residue |
91 |
| 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
|
|
|
30)
|
chain |
A |
| residue |
191 |
| type |
BINDING |
| sequence |
S
|
| 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
|
|
|
31)
|
chain |
A |
| residue |
252 |
| type |
BINDING |
| sequence |
S
|
| 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
|
|
|
32)
|
chain |
A |
| residue |
116 |
| type |
BINDING |
| sequence |
H
|
| 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
|
|
|
33)
|
chain |
A |
| residue |
120 |
| 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
|
|
|
34)
|
chain |
A |
| residue |
122 |
| 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
|
|
|
35)
|
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
|
|
|
36)
|
chain |
A |
| residue |
136 |
| type |
CARBOHYD |
| sequence |
L
|
| 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
|
|
|
|