eF-site ID 6i5c-ABCDEF PDB Code 6i5c Chain A, B, C, D, E, F click to enlarge Title Long wavelength native-SAD phasing of Tubulin-Stathmin-TTL complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source (E1BQ43_CHICK) Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDS B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRALTV PELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEV DEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSAT FIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEM EFTEAESNMNDLVSEYQQYQDA C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPDPSLEEIQKKLEAAEERR KYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKL AQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPREVFLAAYNRRREGREGN VWIAKSSILISSEASELLDFIDEVHVIQKYLEKPLLLEPG HRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQD KTCHLTNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDAL NTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLF GFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAI SSVFPLAPTSIFIKLH Description (1)  Tubulin alpha-1B chain, Tubulin beta-2B chain, Stathmin-4, TUBULIN-TYROSINE LIGASE Functional site 1) chain A residue 10 type sequence G description binding site for residue GTP A 501 source : AC1 2) chain A residue 11 type sequence Q description binding site for residue GTP A 501 source : AC1 3) chain A residue 12 type sequence A description binding site for residue GTP A 501 source : AC1 4) chain A residue 15 type sequence Q description binding site for residue GTP A 501 source : AC1 5) chain A residue 98 type sequence D description binding site for residue GTP A 501 source : AC1 6) chain A residue 99 type sequence A description binding site for residue GTP A 501 source : AC1 7) chain A residue 100 type sequence A description binding site for residue GTP A 501 source : AC1 8) chain A residue 101 type sequence N description binding site for residue GTP A 501 source : AC1 9) chain A residue 140 type sequence S description binding site for residue GTP A 501 source : AC1 10) chain A residue 143 type sequence G description binding site for residue GTP A 501 source : AC1 11) chain A residue 144 type sequence G description binding site for residue GTP A 501 source : AC1 12) chain A residue 145 type sequence T description binding site for residue GTP A 501 source : AC1 13) chain A residue 146 type sequence G description binding site for residue GTP A 501 source : AC1 14) chain A residue 177 type sequence V description binding site for residue GTP A 501 source : AC1 15) chain A residue 183 type sequence E description binding site for residue GTP A 501 source : AC1 16) chain A residue 206 type sequence N description binding site for residue GTP A 501 source : AC1 17) chain A residue 224 type sequence Y description binding site for residue GTP A 501 source : AC1 18) chain A residue 228 type sequence N description binding site for residue GTP A 501 source : AC1 19) chain A residue 231 type sequence I description binding site for residue GTP A 501 source : AC1 20) chain B residue 254 type sequence K description binding site for residue GTP A 501 source : AC1 21) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 22) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 23) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 24) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 25) chain A residue 161 type sequence Y description binding site for residue CL A 504 source : AC4 26) chain A residue 162 type sequence G description binding site for residue CL A 504 source : AC4 27) chain A residue 163 type sequence K description binding site for residue CL A 504 source : AC4 28) chain A residue 164 type sequence K description binding site for residue CL A 504 source : AC4 29) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC5 30) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC5 31) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC5 32) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC5 33) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC5 34) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC5 35) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC5 36) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC5 37) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC5 38) chain B residue 173 type sequence P description binding site for residue GDP B 501 source : AC5 39) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC5 40) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC5 41) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC5 42) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC5 43) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC5 44) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC5 45) chain B residue 113 type sequence E description binding site for residue CA B 502 source : AC6 46) chain C residue 284 type sequence E description binding site for residue CA B 502 source : AC6 47) chain B residue 158 type sequence R description binding site for residue MES B 503 source : AC7 48) chain B residue 162 type sequence P description binding site for residue MES B 503 source : AC7 49) chain B residue 163 type sequence D description binding site for residue MES B 503 source : AC7 50) chain B residue 164 type sequence R description binding site for residue MES B 503 source : AC7 51) chain B residue 197 type sequence N description binding site for residue MES B 503 source : AC7 52) chain B residue 199 type sequence D description binding site for residue MES B 503 source : AC7 53) chain B residue 253 type sequence R description binding site for residue MES B 503 source : AC7 54) chain B residue 296 type sequence F description binding site for residue MES B 504 source : AC8 55) chain B residue 297 type sequence D description binding site for residue MES B 504 source : AC8 56) chain B residue 298 type sequence S description binding site for residue MES B 504 source : AC8 57) chain B residue 306 type sequence D description binding site for residue MES B 504 source : AC8 58) chain B residue 308 type sequence R description binding site for residue MES B 504 source : AC8 59) chain B residue 339 type sequence N description binding site for residue MES B 504 source : AC8 60) chain B residue 342 type sequence Y description binding site for residue MES B 504 source : AC8 61) chain B residue 11 type sequence Q description binding site for residue CA B 505 source : AC9 62) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AD1 63) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AD1 64) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AD1 65) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AD1 66) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AD1 67) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AD1 68) chain C residue 100 type sequence A description binding site for residue GTP C 501 source : AD1 69) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AD1 70) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AD1 71) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AD1 72) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AD1 73) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AD1 74) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AD1 75) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AD1 76) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AD1 77) chain C residue 179 type sequence T description binding site for residue GTP C 501 source : AD1 78) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AD1 79) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AD1 80) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AD1 81) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AD1 82) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AD1 83) chain D residue 254 type sequence K description binding site for residue GTP C 501 source : AD1 84) chain C residue 11 type sequence Q description binding site for residue MG C 502 source : AD2 85) chain C residue 69 type sequence D description binding site for residue MG C 502 source : AD2 86) chain C residue 71 type sequence E description binding site for residue MG C 502 source : AD2 87) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD3 88) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD3 89) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD3 90) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD3 91) chain C residue 233 type sequence Q description binding site for residue CL C 504 source : AD4 92) chain C residue 362 type sequence V description binding site for residue CL C 504 source : AD4 93) chain C residue 363 type sequence V description binding site for residue CL C 504 source : AD4 94) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AD5 95) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AD5 96) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AD5 97) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AD5 98) chain D residue 140 type sequence S description binding site for residue GDP D 501 source : AD5 99) chain D residue 143 type sequence G description binding site for residue GDP D 501 source : AD5 100) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AD5 101) chain D residue 145 type sequence T description binding site for residue GDP D 501 source : AD5 102) chain D residue 146 type sequence G description binding site for residue GDP D 501 source : AD5 103) chain D residue 178 type sequence S description binding site for residue GDP D 501 source : AD5 104) chain D residue 183 type sequence E description binding site for residue GDP D 501 source : AD5 105) chain D residue 206 type sequence N description binding site for residue GDP D 501 source : AD5 106) chain D residue 209 type sequence L description binding site for residue GDP D 501 source : AD5 107) chain D residue 224 type sequence Y description binding site for residue GDP D 501 source : AD5 108) chain D residue 228 type sequence N description binding site for residue GDP D 501 source : AD5 109) chain D residue 11 type sequence Q description binding site for residue CA D 502 source : AD6 110) chain D residue 101 type sequence N description binding site for residue CA D 502 source : AD6 111) chain F residue 202 type sequence R description binding site for residue MG F 401 source : AD7 112) chain F residue 222 type sequence R description binding site for residue MG F 401 source : AD7 113) chain F residue 318 type sequence D description binding site for residue MG F 401 source : AD7 114) chain F residue 331 type sequence E description binding site for residue MG F 401 source : AD7 115) chain F residue 333 type sequence N description binding site for residue MG F 401 source : AD7 116) chain F residue 74 type sequence K description binding site for residue ACP F 402 source : AD8 117) chain F residue 150 type sequence K description binding site for residue ACP F 402 source : AD8 118) chain F residue 183 type sequence Q description binding site for residue ACP F 402 source : AD8 119) chain F residue 184 type sequence K description binding site for residue ACP F 402 source : AD8 120) chain F residue 185 type sequence Y description binding site for residue ACP F 402 source : AD8 121) chain F residue 186 type sequence L description binding site for residue ACP F 402 source : AD8 122) chain F residue 198 type sequence K description binding site for residue ACP F 402 source : AD8 123) chain F residue 239 type sequence H description binding site for residue ACP F 402 source : AD8 124) chain F residue 241 type sequence T description binding site for residue ACP F 402 source : AD8 125) chain F residue 242 type sequence N description binding site for residue ACP F 402 source : AD8 126) chain F residue 330 type sequence I description binding site for residue ACP F 402 source : AD8 127) chain F residue 331 type sequence E description binding site for residue ACP F 402 source : AD8 128) chain F residue 333 type sequence N description binding site for residue ACP F 402 source : AD8 129) 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_FI10 130) 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_FI10 131) 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_FI9 132) 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_FI9 133) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 134) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 135) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 136) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 137) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 138) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 139) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 140) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 141) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 142) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 143) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 144) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 145) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 146) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 147) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 148) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 149) chain E residue 19 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 163) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 164) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 165) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 166) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 167) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 168) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 169) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 170) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 171) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 172) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 173) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 174) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 175) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 176) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 177) chain C residue 48 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 178) chain C residue 232 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 179) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 180) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 181) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 182) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 183) chain A residue 370 type MOD_RES sequence K description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 184) chain C residue 326 type MOD_RES sequence K description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 185) chain C residue 370 type MOD_RES sequence K description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

Display surface Download Links