eF-site ID 5c08-ABCDEFGHIJ PDB Code 5c08 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title 1E6 TCR in Complex with HLA-A0e carrying RQWGPDPAAV Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5C08) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  RQWGPDPAAV D:  EVEQDPGPLSVPEGAIVSLNCTYSNSAFQYFMWYRQYSRK GPELLMYTYSSGNKEDGRFTAQVDKSSKYISLFIRDSQPS DSATYLCAMRGDSSYKLIFGSGTRLLVRPDIQNPDPAVYQ LRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLD MRSMDFKSNSAVAWSNKSDFACANAFNNS E:  GVIQSPRHEVTEMGQQVTLRCKPISGHDYLFWYRQTMMRG LELLIYFNNNVPIDDSGMPEDRFSAKMPNASFSTLKIQPS EPRDSAVYFCASSLWEKLAKNIQYFGAGTRLSVLEDLKNV FPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWW VNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATF WQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAW GRAD F:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP G:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM H:  RQWGPDPAAV I:  AEVEQDPGPLSVPEGAIVSLNCTYSNSAFQYFMWYRQYSR KGPELLMYTYSSGNKEDGRFTAQVDKSSKYISLFIRDSQP SDSATYLCAMRGDSSYKLIFGSGTRLLVRPDIQNPDPAVY QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL DMRSMDFKSNSAVAWSNKSDFACANAFNNSI J:  AGVIQSPRHEVTEMGQQVTLRCKPISGHDYLFWYRQTMMR GLELLIYFNNNVPIDDSGMPEDRFSAKMPNASFSTLKIQP SEPRDSAVYFCASSLWEKLAKNIQYFGAGTRLSVLEDLKN VFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSW WVNGKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSAT FWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEA WGRAD Description Functional site 1) chain A residue 21 type sequence R description binding site for residue EDO A 301 source : AC1 2) chain B residue 51 type sequence H description binding site for residue EDO A 301 source : AC1 3) chain A residue 85 type sequence Y description binding site for residue EDO A 302 source : AC2 4) chain A residue 87 type sequence Q description binding site for residue EDO A 302 source : AC2 5) chain A residue 118 type sequence Y description binding site for residue EDO A 302 source : AC2 6) chain A residue 119 type sequence D description binding site for residue EDO A 302 source : AC2 7) chain A residue 121 type sequence K description binding site for residue EDO A 302 source : AC2 8) chain B residue 0 type sequence M description binding site for residue EDO A 302 source : AC2 9) chain A residue 4 type sequence S description binding site for residue GOL A 303 source : AC3 10) chain A residue 6 type sequence R description binding site for residue GOL A 303 source : AC3 11) chain A residue 8 type sequence F description binding site for residue GOL A 303 source : AC3 12) chain A residue 27 type sequence Y description binding site for residue GOL A 303 source : AC3 13) chain A residue 29 type sequence D description binding site for residue GOL A 303 source : AC3 14) chain A residue 234 type sequence R description binding site for residue EDO B 301 source : AC4 15) chain A residue 242 type sequence Q description binding site for residue EDO B 301 source : AC4 16) chain B residue 11 type sequence S description binding site for residue EDO B 301 source : AC4 17) chain B residue 13 type sequence H description binding site for residue EDO B 301 source : AC4 18) chain B residue 14 type sequence P description binding site for residue EDO B 301 source : AC4 19) chain B residue 99 type sequence M description binding site for residue EDO B 301 source : AC4 20) chain B residue 45 type sequence R description binding site for residue EDO B 302 source : AC5 21) chain B residue 47 type sequence E description binding site for residue EDO B 302 source : AC5 22) chain B residue 48 type sequence K description binding site for residue EDO B 302 source : AC5 23) chain J residue 220 type sequence S description binding site for residue EDO B 302 source : AC5 24) chain J residue 221 type sequence E description binding site for residue EDO B 302 source : AC5 25) chain J residue 231 type sequence K description binding site for residue EDO B 302 source : AC5 26) chain A residue 23 type sequence I description binding site for residue EDO B 303 source : AC6 27) chain A residue 35 type sequence R description binding site for residue EDO B 303 source : AC6 28) chain A residue 37 type sequence D description binding site for residue EDO B 303 source : AC6 29) chain B residue 51 type sequence H description binding site for residue EDO B 303 source : AC6 30) chain B residue 52 type sequence S description binding site for residue EDO B 303 source : AC6 31) chain B residue 53 type sequence D description binding site for residue EDO B 303 source : AC6 32) chain B residue 54 type sequence L description binding site for residue EDO B 303 source : AC6 33) chain A residue 146 type sequence K description binding site for residue EDO C 101 source : AC7 34) chain C residue 9 type sequence A description binding site for residue EDO C 101 source : AC7 35) chain E residue 97 type sequence W description binding site for residue EDO C 101 source : AC7 36) chain E residue 98 type sequence E description binding site for residue EDO C 101 source : AC7 37) chain D residue 77 type sequence R description binding site for residue EDO D 201 source : AC8 38) chain I residue 77 type sequence R description binding site for residue EDO D 201 source : AC8 39) chain D residue 60 type sequence R description binding site for residue GOL D 202 source : AC9 40) chain D residue 61 type sequence F description binding site for residue GOL D 202 source : AC9 41) chain D residue 49 type sequence Y description binding site for residue SO4 D 203 source : AD1 42) chain D residue 56 type sequence K description binding site for residue SO4 D 203 source : AD1 43) chain D residue 5 type sequence E description binding site for residue SO4 D 204 source : AD2 44) chain D residue 7 type sequence D description binding site for residue SO4 D 204 source : AD2 45) chain D residue 22 type sequence N description binding site for residue SO4 D 204 source : AD2 46) chain D residue 23 type sequence C description binding site for residue SO4 D 204 source : AD2 47) chain D residue 24 type sequence T description binding site for residue SO4 D 204 source : AD2 48) chain E residue 164 type sequence N description binding site for residue EDO E 301 source : AD3 49) chain E residue 165 type sequence G description binding site for residue EDO E 301 source : AD3 50) chain E residue 211 type sequence R description binding site for residue EDO E 301 source : AD3 51) chain G residue 88 type sequence S description binding site for residue EDO E 301 source : AD3 52) chain E residue 22 type sequence R description binding site for residue EDO E 302 source : AD4 53) chain E residue 74 type sequence F description binding site for residue EDO E 302 source : AD4 54) chain F residue 17 type sequence R description binding site for residue EDO E 302 source : AD4 55) chain F residue 18 type sequence G description binding site for residue EDO E 302 source : AD4 56) chain E residue 84 type sequence P description binding site for residue EDO E 303 source : AD5 57) chain E residue 85 type sequence R description binding site for residue EDO E 303 source : AD5 58) chain D residue 34 type sequence M description binding site for residue EDO E 304 source : AD6 59) chain D residue 36 type sequence Y description binding site for residue EDO E 304 source : AD6 60) chain D residue 92 type sequence R description binding site for residue EDO E 304 source : AD6 61) chain D residue 97 type sequence Y description binding site for residue EDO E 304 source : AD6 62) chain D residue 99 type sequence L description binding site for residue EDO E 304 source : AD6 63) chain E residue 103 type sequence N description binding site for residue EDO E 304 source : AD6 64) chain E residue 105 type sequence Q description binding site for residue EDO E 304 source : AD6 65) chain E residue 8 type sequence P description binding site for residue EDO E 305 source : AD7 66) chain E residue 9 type sequence R description binding site for residue EDO E 305 source : AD7 67) chain E residue 10 type sequence H description binding site for residue EDO E 305 source : AD7 68) chain A residue 73 type sequence T description binding site for residue GOL E 306 source : AD8 69) chain C residue 7 type sequence P description binding site for residue GOL E 306 source : AD8 70) chain C residue 9 type sequence A description binding site for residue GOL E 306 source : AD8 71) chain E residue 30 type sequence D description binding site for residue GOL E 306 source : AD8 72) chain E residue 31 type sequence Y description binding site for residue GOL E 306 source : AD8 73) chain E residue 50 type sequence N description binding site for residue GOL E 306 source : AD8 74) chain E residue 51 type sequence N description binding site for residue GOL E 306 source : AD8 75) chain A residue 68 type sequence K description binding site for residue SO4 E 307 source : AD9 76) chain E residue 54 type sequence P description binding site for residue SO4 E 307 source : AD9 77) chain E residue 55 type sequence I description binding site for residue SO4 E 307 source : AD9 78) chain E residue 57 type sequence D description binding site for residue SO4 E 307 source : AD9 79) chain E residue 57 type sequence D description binding site for residue SO4 E 308 source : AE1 80) chain E residue 66 type sequence S description binding site for residue SO4 E 308 source : AE1 81) chain E residue 67 type sequence A description binding site for residue SO4 E 308 source : AE1 82) chain F residue 4 type sequence S description binding site for residue EDO F 301 source : AE2 83) chain F residue 6 type sequence R description binding site for residue EDO F 301 source : AE2 84) chain F residue 29 type sequence D description binding site for residue EDO F 301 source : AE2 85) chain F residue 73 type sequence T description binding site for residue EDO F 302 source : AE3 86) chain J residue 31 type sequence Y description binding site for residue EDO F 302 source : AE3 87) chain J residue 50 type sequence N description binding site for residue EDO F 302 source : AE3 88) chain J residue 97 type sequence W description binding site for residue EDO F 302 source : AE3 89) chain F residue 116 type sequence Y description binding site for residue EDO F 303 source : AE4 90) chain F residue 122 type sequence D description binding site for residue EDO F 303 source : AE4 91) chain F residue 123 type sequence Y description binding site for residue EDO F 303 source : AE4 92) chain F residue 124 type sequence I description binding site for residue EDO F 303 source : AE4 93) chain F residue 125 type sequence A description binding site for residue EDO F 303 source : AE4 94) chain G residue 60 type sequence W description binding site for residue EDO F 303 source : AE4 95) chain F residue 14 type sequence R description binding site for residue EDO F 304 source : AE5 96) chain F residue 17 type sequence R description binding site for residue EDO F 304 source : AE5 97) chain F residue 21 type sequence R description binding site for residue EDO F 304 source : AE5 98) chain G residue 34 type sequence D description binding site for residue EDO F 304 source : AE5 99) chain F residue 48 type sequence R description binding site for residue SO4 F 305 source : AE6 100) chain F residue 49 type sequence A description binding site for residue SO4 F 305 source : AE6 101) chain F residue 50 type sequence P description binding site for residue SO4 F 305 source : AE6 102) chain F residue 53 type sequence E description binding site for residue SO4 F 305 source : AE6 103) chain F residue 37 type sequence D description binding site for residue EDO G 101 source : AE7 104) chain G residue 51 type sequence H description binding site for residue EDO G 101 source : AE7 105) chain G residue 52 type sequence S description binding site for residue EDO G 101 source : AE7 106) chain G residue 53 type sequence D description binding site for residue EDO G 101 source : AE7 107) chain G residue 54 type sequence L description binding site for residue EDO G 101 source : AE7 108) chain D residue 69 type sequence S description binding site for residue EDO I 201 source : AE8 109) chain D residue 71 type sequence Y description binding site for residue EDO I 201 source : AE8 110) chain I residue 10 type sequence P description binding site for residue EDO I 201 source : AE8 111) chain I residue 12 type sequence S description binding site for residue EDO I 201 source : AE8 112) chain I residue 47 type sequence L description binding site for residue EDO I 202 source : AE9 113) chain I residue 48 type sequence M description binding site for residue EDO I 202 source : AE9 114) chain I residue 58 type sequence D description binding site for residue EDO I 202 source : AE9 115) chain I residue 59 type sequence G description binding site for residue EDO I 203 source : AF1 116) chain I residue 60 type sequence R description binding site for residue EDO I 203 source : AF1 117) chain I residue 61 type sequence F description binding site for residue EDO I 203 source : AF1 118) chain D residue 10 type sequence P description binding site for residue EDO I 204 source : AF2 119) chain D residue 12 type sequence S description binding site for residue EDO I 204 source : AF2 120) chain I residue 69 type sequence S description binding site for residue EDO I 204 source : AF2 121) chain I residue 71 type sequence Y description binding site for residue EDO I 204 source : AF2 122) chain D residue 71 type sequence Y description binding site for residue EDO I 205 source : AF3 123) chain I residue 13 type sequence V description binding site for residue EDO I 205 source : AF3 124) chain I residue 18 type sequence I description binding site for residue EDO I 205 source : AF3 125) chain I residue 19 type sequence V description binding site for residue EDO I 205 source : AF3 126) chain I residue 20 type sequence S description binding site for residue EDO I 205 source : AF3 127) chain J residue 41 type sequence R description binding site for residue EDO J 301 source : AF4 128) chain J residue 60 type sequence M description binding site for residue EDO J 301 source : AF4 129) chain J residue 61 type sequence P description binding site for residue EDO J 301 source : AF4 130) chain I residue 92 type sequence R description binding site for residue EDO J 302 source : AF5 131) chain I residue 97 type sequence Y description binding site for residue EDO J 302 source : AF5 132) chain I residue 99 type sequence L description binding site for residue EDO J 302 source : AF5 133) chain J residue 100 type sequence L description binding site for residue EDO J 302 source : AF5 134) chain J residue 103 type sequence N description binding site for residue EDO J 302 source : AF5 135) chain J residue 105 type sequence Q description binding site for residue EDO J 302 source : AF5 136) chain J residue 36 type sequence R description binding site for residue EDO J 303 source : AF6 137) chain J residue 64 type sequence R description binding site for residue EDO J 303 source : AF6 138) chain J residue 65 type sequence F description binding site for residue EDO J 303 source : AF6 139) chain J residue 86 type sequence D description binding site for residue EDO J 303 source : AF6 140) chain J residue 85 type sequence R description binding site for residue SO4 J 304 source : AF7 141) chain J residue 102 type sequence K description binding site for residue SO4 J 304 source : AF7 142) chain J residue 104 type sequence I description binding site for residue SO4 J 305 source : AF8 143) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH source prosite : PS00290 144) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH source prosite : PS00290 145) chain E residue 71 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 146) chain F residue 143 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 147) chain F residue 146 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 148) chain F residue 171 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 149) chain J residue 71 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 150) chain A residue 84 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 151) chain A residue 143 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 152) chain A residue 146 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 153) chain A residue 171 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 154) chain F residue 7 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 155) chain F residue 73 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 156) chain F residue 84 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 157) chain E residue 186 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI2 158) chain J residue 186 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI2 159) chain I residue 144 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI2 160) chain I residue 178 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI2 161) chain D residue 189 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 162) chain G residue 58 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 163) chain G residue 91 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 164) chain G residue 94 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 165) chain I residue 189 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 166) chain B residue 48 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 167) chain B residue 58 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 168) chain B residue 91 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 169) chain B residue 94 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 170) chain G residue 19 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 171) chain G residue 41 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 172) chain G residue 48 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI3 173) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 174) chain F residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4

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