eF-site ID 3du7-ABCDE PDB Code 3du7 Chain A, B, C, D, E click to enlarge Title Tubulin-colchicine-phomopsin A: Stathmin-like domain complex Classification CELL CYCLE Compound Tubulin alpha-1C chain Source ORGANISM_COMMON: bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSFNT FFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQ LISGKEDAANNYARGHYTIGKEIIDLVLDRVRKLADQCTG LQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSI YPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYD ICRRNLDIERPTYTNLNRLMSQIVSSITASLRFDGALNVD LTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEI TNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAA IATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKV QRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGE GMEEGEFSEAREDMAALEKDYEEVGADS B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYS IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAVFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQD C:  RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKT IGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG TYRQLFHPEQLISGKEDAANNYARGHYTIGKEIIDLVLDR VRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDY GKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCA FMVDNEAIYDICRRNLDIERPTYTNLNRLMSQIVSSITAS LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKA YHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRG DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPT VVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAK RAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADS D:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYS IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAVFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQD E:  ADMEVIELNKCTSGQSFEVILKPPSSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK E Description Functional site 1) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE MG A 500 source : AC1 2) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE MG A 500 source : AC1 3) chain A residue 101 type sequence N description BINDING SITE FOR RESIDUE MG A 500 source : AC1 4) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE MG A 500 source : AC1 5) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE MG A 500 source : AC1 6) chain C residue 98 type sequence D description BINDING SITE FOR RESIDUE MG C 501 source : AC2 7) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE MG C 501 source : AC2 8) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE MG C 501 source : AC2 9) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 10) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 11) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 12) chain A residue 69 type sequence D description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 13) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 14) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 15) chain A residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 16) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 17) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 18) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 19) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 20) chain A residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 21) chain A residue 173 type sequence P description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 22) chain A residue 178 type sequence S description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 23) chain A residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 24) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 25) chain A residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 26) chain A residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP D 600 source : AC3 27) chain C residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 28) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 29) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 30) chain C residue 16 type sequence I description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 31) chain C residue 71 type sequence E description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 32) chain C residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 33) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 34) chain C residue 142 type sequence G description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 35) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 36) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 37) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 38) chain C residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 39) chain C residue 173 type sequence P description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 40) chain C residue 178 type sequence S description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 41) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 42) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 43) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 44) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 45) chain C residue 231 type sequence M description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 46) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP D 601 source : AC4 47) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 48) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 49) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 50) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 51) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 52) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 53) chain B residue 173 type sequence P description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 54) chain B residue 178 type sequence S description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 55) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 56) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 57) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 58) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 59) chain D residue 10 type sequence G description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 60) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 61) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 62) chain D residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 63) chain D residue 142 type sequence G description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 64) chain D residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 65) chain D residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 66) chain D residue 173 type sequence P description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 67) chain D residue 178 type sequence S description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 68) chain D residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 69) chain D residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 70) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 71) chain D residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 603 source : AC6 72) chain A residue 178 type sequence S description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 73) chain A residue 179 type sequence T description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 74) chain A residue 180 type sequence A description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 75) chain B residue 241 type sequence C description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 76) chain B residue 242 type sequence L description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 77) chain B residue 250 type sequence A description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 78) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 79) chain B residue 255 type sequence L description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 80) chain B residue 258 type sequence N description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 81) chain B residue 259 type sequence M description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 82) chain B residue 316 type sequence A description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 83) chain B residue 352 type sequence K description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 84) chain C residue 178 type sequence S description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 85) chain C residue 180 type sequence A description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 86) chain D residue 241 type sequence C description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 87) chain D residue 242 type sequence L description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 88) chain D residue 250 type sequence A description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 89) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 90) chain D residue 255 type sequence L description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 91) chain D residue 258 type sequence N description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 92) chain D residue 259 type sequence M description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 93) chain D residue 316 type sequence A description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 94) chain D residue 352 type sequence K description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 95) chain D residue 378 type sequence I description BINDING SITE FOR RESIDUE CN2 D 701 source : AC8 96) chain B residue 178 type sequence S description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 97) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 98) chain B residue 222 type sequence P description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 99) chain B residue 223 type sequence T description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 100) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 101) chain C residue 325 type sequence P description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 102) chain C residue 329 type sequence N description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 103) chain C residue 351 type sequence F description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 104) chain D residue 37 type sequence H description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 105) chain D residue 178 type sequence S description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 106) chain D residue 179 type sequence D description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 107) chain D residue 210 type sequence Y description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 108) chain D residue 221 type sequence T description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 109) chain D residue 222 type sequence P description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 110) chain D residue 223 type sequence T description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 111) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE HOS D 801 source : BC1 112) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 113) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 114) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 115) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 116) chain B residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 117) chain D residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 118) chain B residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI11 119) chain D residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI11 120) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 121) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 122) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 123) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 124) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 125) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 126) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 127) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 128) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 129) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 130) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 131) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 132) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 133) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 134) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 135) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 136) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 137) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 138) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 139) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 140) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 141) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 142) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 143) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 144) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 145) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 146) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 147) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 148) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 149) chain E residue 46 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 150) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 151) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 152) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 153) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 154) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 155) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 156) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 157) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 158) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 159) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 160) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 161) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 162) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links