eF-site ID 1blf-A PDB Code 1blf Chain A click to enlarge Title STRUCTURE OF DIFERRIC BOVINE LACTOFERRIN AT 2.8 ANGSTROMS RESOLUTION Classification IRON-BINDING PROTEIN Compound LACTOFERRIN Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  NVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALE CIRAIAEKKADAVTLDGGMVFEAGRDPYKLRPVAAEIYGT KESPQTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRSAG WIIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPCIDRQ AYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAG DVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKE CHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSR SFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYLGSRY LTTLKNLRETAEEVKARYTRVVWCAVGPEEQKKCQQWSQQ SGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGK CGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANE GLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVNQTGSCAFD EFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYY GYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNL NREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRA AHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDN TECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEAC AFLTR Description Functional site 1) chain A residue 60 type sequence D description FE+3 BINDING SITE. source : FE1 2) chain A residue 92 type sequence Y description FE+3 BINDING SITE. source : FE1 3) chain A residue 192 type sequence Y description FE+3 BINDING SITE. source : FE1 4) chain A residue 253 type sequence H description FE+3 BINDING SITE. source : FE1 5) chain A residue 395 type sequence D description FE+3 BINDING SITE. source : FE2 6) chain A residue 433 type sequence Y description FE+3 BINDING SITE. source : FE2 7) chain A residue 526 type sequence Y description FE+3 BINDING SITE. source : FE2 8) chain A residue 595 type sequence H description FE+3 BINDING SITE. source : FE2 9) chain A residue 92-101 type prosite sequence YYAVAVVKKG description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG source prosite : PS00205 10) chain A residue 433-442 type prosite sequence YLAVAVVKKA description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG source prosite : PS00205 11) chain A residue 192-208 type prosite sequence YSGAFKCLQDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF source prosite : PS00206 12) chain A residue 526-542 type prosite sequence YTGAFRCLAEDVGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF source prosite : PS00206 13) chain A residue 226-256 type prosite sequence QYELLCLNNSRAPVDAFKECHLAQVPSHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNnsrap...VdafkeChlAqvpsHaVV source prosite : PS00207 14) chain A residue 568-598 type prosite sequence DFRLLCLDGTRKPVTEAQSCHLAVAPNHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNnsrap...VdafkeChlAqvpsHaVV source prosite : PS00207 15) chain A residue 73 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 259 type ACT_SITE sequence S description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF source Swiss-Prot : SWS_FT_FI3 18) chain A residue 92 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF source Swiss-Prot : SWS_FT_FI3 19) chain A residue 192 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF source Swiss-Prot : SWS_FT_FI3 20) chain A residue 253 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF source Swiss-Prot : SWS_FT_FI3 21) 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_FI3 22) 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_FI3 23) 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_FI3 24) 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_FI3 25) chain A residue 117 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 123 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 124 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 459 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 463 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 465 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 466 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI4 33) 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.2021.104999 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 281 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999 source Swiss-Prot : SWS_FT_FI6 35) 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_FI7 36) 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_FI7 37) 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_FI8

Display surface Download Links