eF-site ID 1i6q-A PDB Code 1i6q Chain A click to enlarge Title Formation of a protein intermediate and its trapping by the simultaneous crystallization process: Crystal structure of an iron-saturated intermediate in the FE3+ binding pathway of camel lactoferrin at 2.7 resolution Classification METAL TRANSPORT Compound LACTOFERRIN Source ORGANISM_COMMON: Arabian camel; ORGANISM_SCIENTIFIC: Camelus dromedarius; Sequence A:  ASKKSVRWCTTSPAESKKCAQWQRRMKKVRGPSVTCVKKT SRFECIQAISTEKADAVTLDGGLVYDAGLDPYKLRPIAAE VYGTENQPQTHYYAVAIAKKGTNFQLNQLQGLKSCHTGLG RSAGWNIPMGLLRPFLDWTGPPEPLQKAVAKFFSASCVPC VDGKEYPNLCQLCAGTGENKCACSSQEPYFGYSGAFKCLQ DGAGDVAFVKDSTVFESLPAKADRDQYELLCPNNTRKPVD AFQECHLARVPSHAVVARSVNGKEDLIWKLLVKAQEKFGR GKPSAFQLFGSPAGQKDLLFKDSALGLLRIPKKIDSGLYL GSNYITAIRGLRETAAEVELRRAQVVWCAVGSDEQLKCQE WSRQSNQSVVCATASTTEDCIALVLKGEADALSLDGGYIY IAGKCGLVPVLAESQQSPESSGLDCVHRPVKGYLAVAVVR KANDKITWNSLRGKKSCHTAVDRTAGWNIPMGPLFKDTDS CRFDEFFSQSCAPGSDPRSKLCALCAGNEEGQLKCVPNSS ERLYGYTGAFRCLAENVGDVAFVKDVTVLDNTDGKGTEQW AKDLKLGDFELLCLNGTRKPVTEAESCHLPVAPNHAVVSR IDKVAHLRQVLLRQQAHFGRNGEDCPGKFCLFQSKTKNLL FNDNTECLAKLQGKTTYDEYLGPQYVTAIAKLRRCSTSPL LEACAFLMR Description Functional site 1) chain A residue 92 type sequence Y description BINDING SITE FOR RESIDUE FE A 690 source : AC1 2) chain A residue 122 type sequence S description BINDING SITE FOR RESIDUE FE A 690 source : AC1 3) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE FE A 690 source : AC1 4) chain A residue 463 type sequence R description BINDING SITE FOR RESIDUE FE A 691 source : AC2 5) chain A residue 526 type sequence Y description BINDING SITE FOR RESIDUE FE A 691 source : AC2 6) chain A residue 121 type sequence R description BINDING SITE FOR RESIDUE CO3 A 692 source : AC3 7) chain A residue 463 type sequence R description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 8) chain A residue 464 type sequence T description BINDING SITE FOR RESIDUE CO3 A 693 source : AC4 9) chain A residue 73 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 259 type ACT_SITE sequence S description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 92-101 type prosite sequence YYAVAIAKKG description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAIAKKG source prosite : PS00205 12) chain A residue 433-442 type prosite sequence YLAVAVVRKA description TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAIAKKG source prosite : PS00205 13) chain A residue 192-208 type prosite sequence YSGAFKCLQDGAGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF source prosite : PS00206 14) chain A residue 526-542 type prosite sequence YTGAFRCLAENVGDVAF description TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF source prosite : PS00206 15) chain A residue 226-256 type prosite sequence QYELLCPNNTRKPVDAFQECHLARVPSHAVV description TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLCpNntrkp...VdafqeChlArvpsHaVV source prosite : PS00207 16) chain A residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 595 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 117 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 123 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 124 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 253 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 395 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 459 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 465 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 466 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 92 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 192 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 433 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 463 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 526 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:11473113 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 233 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11397094 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 518 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11397094 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 366 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 575 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links