eF-site ID 1d0n-A PDB Code 1d0n Chain A click to enlarge Title THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN. Classification CONTRACTILE PROTEIN Compound HORSE PLASMA GELSOLIN Source ORGANISM_COMMON: horse; ORGANISM_SCIENTIFIC: Equus caballus; Sequence A:  VEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGD AYVILKTVQLRNGILQYDLHYWLGNECSQDESGAAAIFTV QLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVA SGFKHVVPNEVVVQRLLQVKGRRVVRATEVPVSWESFNNG DCFILDLGNNIYQWCGSKSNRFERLKATQVSKGIRDNERS GRAQVSVFEEGAEPEAMLQVLGPKPTLPEATEDTVKEDAA NRKLAKLYKVSNGAGPMVVSLVADENPFAQGALRSEDCFI LDHGKDGKIFVWKGKQANMEERKAALKTASDFISKMDYPK QTQVSVLPEGGETPLFRQFFKNWRDPDQTEGLGLAYLSSH IAHVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRVE GSNKVPVDPATYGQFYGGDSYIILYNYRHGSRQGQIIYNW QGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPA HLMSLFGGKPMIVYKGGTSREGGQTAPASTRLFQVRASSS GATRAVEIIPKAGALNSNDAFVLKTPSAAYLWVGAGASEA EKTGAQELLRVLRAQPVQVAEGSEPDSFWEALGGKATYRT SPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGEFMQEDL ATDDVMLLDTWDQVFVWVGKDSQDEEKTEALTSAKRYIDT DPAHRDRRTPITVVKQGFEPPSFVGWFLGWDDSYWSVDPL DRALAELAA Description (1)  HORSE PLASMA GELSOLIN Functional site 1) chain A residue 558 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P13020 source Swiss-Prot : SWS_FT_FI5 2) chain A residue 716 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI6 3) chain A residue 66 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 4) chain A residue 328 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 5) chain A residue 67 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 6) chain A residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 7) chain A residue 110 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 8) chain A residue 115 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 9) chain A residue 117 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 10) chain A residue 146 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 11) chain A residue 303 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 12) chain A residue 304 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 13) chain A residue 136 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 162 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 495 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 525 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 565 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 566 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 588 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 670 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 671 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 693 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 210 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 260 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 445 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 446 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 476 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 488 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 493 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 187 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 188 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 439 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 577 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 625 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 60 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 383 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4

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