eF-site ID 5lov-ABCDEF PDB Code 5lov Chain A, B, C, D, E, F click to enlarge Title DZ-2384 tubulin complex Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSTVPEL TQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQ MLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIG NSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFT EAESNMNDLVSEYQQYQ C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRFVDWCPTGFKVGINYQPPTVV PGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRA FVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTLTVPEL TQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQ MLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIG NSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFT EAESNMNDLVSEYQQYQDATAD E:  VIELNKCTSGQSFEVILKPDPSLEEIQKKLEAAEERRKYQ EAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQK MESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTTDEREVFLAAYNRGNVW IAISSEASELLDVIQKYLEKPLLLEPGHRKFDIRSWVLVD HLYNIYLYREGVLRTPYNSANYGEEGNEMFFEEFNQYLMD ALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQ LFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDV AISSVFPLATSIFIKLHH Description 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 71 type sequence E description binding site for residue MG A 502 source : AC2 22) chain A residue 98 type sequence D description binding site for residue MG A 502 source : AC2 23) chain B residue 254 type sequence K description binding site for residue MG A 502 source : AC2 24) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 25) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 26) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 27) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 28) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC4 29) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC4 30) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC4 31) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC4 32) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC4 33) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC4 34) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 35) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC4 36) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC4 37) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC4 38) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC4 39) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC4 40) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC4 41) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC4 42) chain B residue 158 type sequence R description binding site for residue MES B 502 source : AC5 43) chain B residue 162 type sequence P description binding site for residue MES B 502 source : AC5 44) chain B residue 163 type sequence D description binding site for residue MES B 502 source : AC5 45) chain B residue 164 type sequence R description binding site for residue MES B 502 source : AC5 46) chain B residue 165 type sequence I description binding site for residue MES B 502 source : AC5 47) chain B residue 197 type sequence N description binding site for residue MES B 502 source : AC5 48) chain B residue 199 type sequence D description binding site for residue MES B 502 source : AC5 49) chain B residue 253 type sequence R description binding site for residue MES B 502 source : AC5 50) chain B residue 11 type sequence Q description binding site for residue MG B 503 source : AC6 51) chain C residue 254 type sequence E description binding site for residue MG B 503 source : AC6 52) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC7 53) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC7 54) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC7 55) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC7 56) chain C residue 16 type sequence I description binding site for residue GTP C 501 source : AC7 57) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC7 58) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC7 59) chain C residue 100 type sequence A description binding site for residue GTP C 501 source : AC7 60) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC7 61) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC7 62) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC7 63) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC7 64) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC7 65) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AC7 66) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AC7 67) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AC7 68) chain C residue 179 type sequence T description binding site for residue GTP C 501 source : AC7 69) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AC7 70) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AC7 71) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AC7 72) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AC7 73) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AC7 74) chain D residue 254 type sequence K description binding site for residue GTP C 501 source : AC7 75) chain C residue 69 type sequence D description binding site for residue MG C 502 source : AC8 76) chain B residue 176 type sequence K description binding site for residue 71E C 503 source : AC9 77) chain B residue 177 type sequence V description binding site for residue 71E C 503 source : AC9 78) chain B residue 178 type sequence S description binding site for residue 71E C 503 source : AC9 79) chain B residue 210 type sequence Y description binding site for residue 71E C 503 source : AC9 80) chain B residue 223 type sequence T description binding site for residue 71E C 503 source : AC9 81) chain B residue 224 type sequence Y description binding site for residue 71E C 503 source : AC9 82) chain B residue 225 type sequence G description binding site for residue 71E C 503 source : AC9 83) chain B residue 227 type sequence L description binding site for residue 71E C 503 source : AC9 84) chain C residue 325 type sequence P description binding site for residue 71E C 503 source : AC9 85) chain C residue 328 type sequence V description binding site for residue 71E C 503 source : AC9 86) chain C residue 329 type sequence N description binding site for residue 71E C 503 source : AC9 87) chain C residue 332 type sequence I description binding site for residue 71E C 503 source : AC9 88) chain C residue 336 type sequence K description binding site for residue 71E C 503 source : AC9 89) chain C residue 351 type sequence F description binding site for residue 71E C 503 source : AC9 90) chain C residue 353 type sequence V description binding site for residue 71E C 503 source : AC9 91) chain C residue 355 type sequence I description binding site for residue 71E C 503 source : AC9 92) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AD1 93) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AD1 94) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AD1 95) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AD1 96) chain D residue 101 type sequence N description binding site for residue GDP D 501 source : AD1 97) chain D residue 140 type sequence S description binding site for residue GDP D 501 source : AD1 98) chain D residue 143 type sequence G description binding site for residue GDP D 501 source : AD1 99) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AD1 100) chain D residue 145 type sequence T description binding site for residue GDP D 501 source : AD1 101) chain D residue 146 type sequence G description binding site for residue GDP D 501 source : AD1 102) chain D residue 178 type sequence S description binding site for residue GDP D 501 source : AD1 103) chain D residue 183 type sequence E description binding site for residue GDP D 501 source : AD1 104) chain D residue 206 type sequence N description binding site for residue GDP D 501 source : AD1 105) chain D residue 224 type sequence Y description binding site for residue GDP D 501 source : AD1 106) chain D residue 228 type sequence N description binding site for residue GDP D 501 source : AD1 107) chain F residue 74 type sequence K description binding site for residue ACP F 401 source : AD2 108) chain F residue 183 type sequence Q description binding site for residue ACP F 401 source : AD2 109) chain F residue 184 type sequence K description binding site for residue ACP F 401 source : AD2 110) chain F residue 185 type sequence Y description binding site for residue ACP F 401 source : AD2 111) chain F residue 186 type sequence L description binding site for residue ACP F 401 source : AD2 112) chain F residue 198 type sequence K description binding site for residue ACP F 401 source : AD2 113) chain F residue 200 type sequence D description binding site for residue ACP F 401 source : AD2 114) chain F residue 320 type sequence M description binding site for residue ACP F 401 source : AD2 115) chain F residue 331 type sequence E description binding site for residue ACP F 401 source : AD2 116) chain F residue 333 type sequence N description binding site for residue ACP F 401 source : AD2 117) chain A residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 118) chain A residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 119) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 120) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 121) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 122) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 123) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 124) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 125) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 126) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 127) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 128) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 129) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 130) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 131) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 132) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 133) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 134) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 135) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 136) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 137) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 138) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 139) chain E residue 19 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 140) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 141) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 142) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 143) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 145) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 146) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 147) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 148) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 149) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 151) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 152) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 153) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 154) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 155) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 156) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 157) 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 158) 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 159) 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 160) 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 161) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 162) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 163) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 164) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 165) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 166) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 167) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 168) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 169) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 170) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 171) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 172) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 173) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 174) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

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