eF-site ID 2ds9-A
PDB Code 2ds9
Chain A

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Title Structure of the complex of C-terminal lobe of bovine lactoferrin with mannose at 2.8 A resolution
Classification METAL BINDING PROTEIN
Compound Lactotransferrin
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence A:  YTRVVWCAVGPEEQKKCQQWSQQSGQNVTCATASTTDDCI
VLVLKGEADALNLDGGYIYTAGKCGLVPVLAENRKSSKHS
SLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDKKSCHTAV
DRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRL
CALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVA
FVKNDTVWENTNGESTADWAKNLKREDFRLLCLDGTRKPV
TEAQSCHLAVAPNHAVVSRSDRAAHVEQVLLHQQALFGKN
GKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYL
GTEYVTAIANLKKCSLEACAF
Description


Functional site

1) chain A
residue 433-442
type prosite
sequence YLAVAVVKKA
description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlAVAVVKKA
source prosite : PS00205

2) chain A
residue 526-542
type prosite
sequence YTGAFRCLAEDVGDVAF
description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLaedvGDVAF
source prosite : PS00206

3) chain A
residue 568-598
type prosite
sequence DFRLLCLDGTRKPVTEAQSCHLAVAPNHAVV
description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DFrLLClDgtrkp...VteaqsChlAvapnHaVV
source prosite : PS00207

4) chain A
residue 395
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 433
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI1

6) chain A
residue 526
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI1

7) chain A
residue 595
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI1

8) chain A
residue 459
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI2

9) chain A
residue 463
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI2

10) chain A
residue 465
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI2

11) chain A
residue 466
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
source Swiss-Prot : SWS_FT_FI2

12) chain A
residue 545
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI4

13) chain A
residue 368
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI3

14) chain A
residue 476
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF
source Swiss-Prot : SWS_FT_FI3


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