eF-site ID 1qjm-A PDB Code 1qjm Chain A click to enlarge Title Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution Classification LACTOFERRIN Compound LACTOFERRIN Source ORGANISM_COMMON: HORSE; ORGANISM_SCIENTIFIC: EQUUS CABALLUS; Sequence A:  APRKSVRWCTISPAEAAKCAKFQRNMKKVRGPSVSCIRKT SSFECIQAIAANKADAVTLDGGLVYEAGLHPYKLRPVAAE VYQTRGKPQTRYYAVAVVKKGSGFQLNQLQGVKSCHTGLG RSAGWNIPIGTLRPYLNWTGPPEPLQKAVANFFSASCVPC ADGKQYPNLCRLCAGTEADKCACSSQEPYFGYSGAFKCLE NGAGDVAFVKDSTVFENLPDEAERDKYELLCPDNTRKPVD AFKECHLARVPSHAVVARSVDGREDLIWKLLHRAQEEFGR NKSSAFQLFGSTPGEQDLLFKDSALGFVRIPSQIDSGLYL GANYLTATQNLRETAAEVAARRERVVWCAVGPEEERKCKQ WSDVSNRKVACASASTTEECIALVLKGEADALNLDGGFIY VAGKCGLVPVLAENQKSQNSNAPDCVHRPPEGYLAVAVVR KSDADLTWNSLSGKKSCHTGVGRTAAWNIPMGLLFNQTGS CKFDKFFSQSCAPGADPQSSLCALCVGNNENENKCMPNSE ERYYGYTGAFRCLAEKAGDVAFVKDVTVLQNTDGKNSEPW AKDLKQEDFELLCLDGTRKPVAEAESCHLARAPNHAVVSQ SDRAQHLKKVLFLQQDQFGGNGPDCPGKFCLFKSETKNLL FNDNTECLAELQGKTTYEQYLGSEYVTSITNLRRCSSSPL LEACAFLRA Description Functional site 1) chain A residue 60 type sequence D description BINDING SITE FOR RESIDUE SM A 690 source : AC1 2) chain A residue 92 type sequence Y description BINDING SITE FOR RESIDUE SM A 690 source : AC1 3) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE SM A 690 source : AC1 4) chain A residue 253 type sequence H description BINDING SITE FOR RESIDUE SM A 690 source : AC1 5) chain A residue 395 type sequence D description BINDING SITE FOR RESIDUE SM A 691 source : AC2 6) chain A residue 433 type sequence Y description BINDING SITE FOR RESIDUE SM A 691 source : AC2 7) chain A residue 463 type sequence R description BINDING SITE FOR RESIDUE SM A 691 source : AC2 8) chain A residue 526 type sequence Y description BINDING SITE FOR RESIDUE SM A 691 source : AC2 9) chain A residue 595 type sequence H description BINDING SITE FOR RESIDUE SM A 691 source : AC2 10) chain A residue 60 type sequence D description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 11) chain A residue 92 type sequence Y description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 12) chain A residue 121 type sequence R description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 13) chain A residue 122 type sequence S description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 14) chain A residue 123 type sequence A description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 15) chain A residue 124 type sequence G description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 16) chain A residue 395 type sequence D description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 17) chain A residue 433 type sequence Y description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 18) chain A residue 459 type sequence T description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 19) chain A residue 463 type sequence R description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 20) chain A residue 464 type sequence T description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 21) chain A residue 465 type sequence A description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 22) chain A residue 466 type sequence A description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 23) chain A residue 92-101 type prosite sequence YYAVAVVKKG description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG source prosite : PS00205 24) chain A residue 433-442 type prosite sequence YLAVAVVRKS description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG source prosite : PS00205 25) chain A residue 192-208 type prosite sequence YSGAFKCLENGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLengaGDVAF source prosite : PS00206 26) chain A residue 526-542 type prosite sequence YTGAFRCLAEKAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLengaGDVAF source prosite : PS00206 27) chain A residue 226-256 type prosite sequence KYELLCPDNTRKPVDAFKECHLARVPSHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV source prosite : PS00207 28) chain A residue 568-598 type prosite sequence DFELLCLDGTRKPVAEAESCHLARAPNHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV source prosite : PS00207 29) chain A residue 73 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 259 type ACT_SITE sequence S description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 92 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 192 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 253 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 395 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 433 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 526 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 595 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 117 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 123 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 124 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 43) chain A residue 459 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 463 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 465 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 466 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 430 type BINDING sequence P description BINDING => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI5 48) chain A residue 594 type BINDING sequence N description BINDING => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 660 type BINDING sequence Y description BINDING => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 137 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 281 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 476 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links