eF-site ID 1dej-AS PDB Code 1dej Chain A, S click to enlarge Title CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1 Classification CONTRACTILE PROTEIN Compound GELSOLIN Source (ACT8_DICDI) Sequence A:  DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRH TGKDSYVGDEAQSKRGILTLKYPIEXGIVTNWDDMEKIWH HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETF NTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYE GYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAERE IVRDIKEKLAYVALDFEAEMKAYKESSALEKSYELPDGQV ITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDV DIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKI KIIAPPERKYSVWIGGSILASLSTFQQMWISKHEYDESGP SIVHRKCF S:  MGSVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTCLYGDF FTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAA IFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKK GGVASGF Description Functional site 1) chain S residue 43 type sequence G description BINDING SITE FOR RESIDUE CA S 128 source : AC1 2) chain S residue 44 type sequence D description BINDING SITE FOR RESIDUE CA S 128 source : AC1 3) chain S residue 75 type sequence E description BINDING SITE FOR RESIDUE CA S 128 source : AC1 4) chain S residue 123 type sequence V description BINDING SITE FOR RESIDUE CA S 128 source : AC1 5) chain A residue 167 type sequence E description BINDING SITE FOR RESIDUE CA S 129 source : AC2 6) chain S residue 87 type sequence D description BINDING SITE FOR RESIDUE CA S 129 source : AC2 7) chain S residue 92 type sequence G description BINDING SITE FOR RESIDUE CA S 129 source : AC2 8) chain S residue 94 type sequence A description BINDING SITE FOR RESIDUE CA S 129 source : AC2 9) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 10) chain A residue 14 type sequence S description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 11) chain A residue 15 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 12) chain A residue 16 type sequence M description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 13) chain A residue 18 type sequence K description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 14) chain A residue 156 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 15) chain A residue 157 type sequence D description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 16) chain A residue 158 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 17) chain A residue 159 type sequence V description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 18) chain A residue 182 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 19) chain A residue 210 type sequence R description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 20) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 21) chain A residue 214 type sequence E description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 22) chain A residue 301 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 23) chain A residue 302 type sequence G description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 24) chain A residue 303 type sequence T description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 25) chain A residue 305 type sequence M description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 26) chain A residue 306 type sequence F description BINDING SITE FOR RESIDUE ATP A 1376 source : AC4 27) chain A residue 53-63 type prosite sequence YVGDEAQSKRG description ACTINS_1 Actins signature 1. YVGDEAQs.KRG source prosite : PS00406 28) chain A residue 356-364 type prosite sequence WISKHEYDE description ACTINS_2 Actins signature 2. WISKhEYDE source prosite : PS00432 29) chain A residue 104-116 type prosite sequence LLTEAPLNPKANR description ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR source prosite : PS01132 30) chain A residue 54 type MOD_RES sequence V description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 31) chain S residue 44 type MOD_RES sequence D description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 32) chain S residue 75 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 33) chain S residue 87 type MOD_RES sequence D description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 34) chain S residue 92 type MOD_RES sequence G description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 35) chain S residue 94 type MOD_RES sequence A description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 36) chain S residue 123 type MOD_RES sequence V description Phosphotyrosine => ECO:0000269|PubMed:7498488 source Swiss-Prot : SWS_FT_FI1 37) chain S residue 113 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 38) chain S residue 37 type MOD_RES sequence Y description Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links