eF-site ID 1d0n-AB PDB Code 1d0n Chain A, B 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 B:  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 136 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 2) chain A residue 162 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 3) chain B residue 136 type BINDING sequence S description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 162 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 558 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P13020 source Swiss-Prot : SWS_FT_FI5 6) chain B residue 558 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P13020 source Swiss-Prot : SWS_FT_FI5 7) chain A residue 716 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI6 8) chain B residue 716 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI6 9) chain A residue 66 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 10) chain A residue 328 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 11) chain B residue 66 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 12) chain B residue 67 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 13) chain B residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 14) chain B residue 110 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 15) chain B residue 115 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 16) chain B residue 117 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 17) chain B residue 146 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 18) chain B residue 303 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 19) chain B residue 304 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 20) chain A residue 67 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 21) chain B residue 328 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 22) chain A residue 98 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 23) chain A residue 110 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 24) chain A residue 115 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 25) chain A residue 117 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 26) chain A residue 146 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 27) chain A residue 303 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 28) chain A residue 304 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI source Swiss-Prot : SWS_FT_FI1 29) chain A residue 187 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 495 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 525 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 565 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 566 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 588 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 670 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 671 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 693 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 187 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 188 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 188 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 210 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 260 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 445 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 446 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 476 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 488 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 493 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 495 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 525 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 565 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 210 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 566 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 588 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 54) chain B residue 670 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 55) chain B residue 671 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 693 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 260 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 445 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 446 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 60) chain A residue 476 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 488 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 493 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI3 63) chain A residue 60 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 64) chain B residue 625 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 383 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 66) chain A residue 439 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 67) chain A residue 577 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 68) chain A residue 625 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 69) chain B residue 60 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 70) chain B residue 383 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 71) chain B residue 439 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 577 type MOD_RES sequence L description Phosphotyrosine => ECO:0000250|UniProtKB:P06396 source Swiss-Prot : SWS_FT_FI4

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