eF-site ID 5meo-ABC PDB Code 5meo Chain A, B, C click to enlarge Title Human Leukocyte Antigen presenting ILGKFLHRL Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5MEO) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  ILGKFLHRL Description Functional site 1) chain A residue 8 type sequence F description binding site for residue EDO A 301 source : AC1 2) chain A residue 29 type sequence D description binding site for residue EDO A 301 source : AC1 3) chain A residue 188 type sequence H description binding site for residue EDO A 302 source : AC2 4) chain A residue 190 type sequence T description binding site for residue EDO A 302 source : AC2 5) chain A residue 204 type sequence W description binding site for residue EDO A 302 source : AC2 6) chain B residue 98 type sequence D description binding site for residue EDO A 302 source : AC2 7) chain A residue 17 type sequence R description binding site for residue EDO A 303 source : AC3 8) chain A residue 121 type sequence K description binding site for residue EDO A 303 source : AC3 9) chain A residue 14 type sequence R description binding site for residue EDO A 304 source : AC4 10) chain A residue 20 type sequence P description binding site for residue EDO A 304 source : AC4 11) chain A residue 21 type sequence R description binding site for residue EDO A 304 source : AC4 12) chain A residue 38 type sequence S description binding site for residue EDO A 304 source : AC4 13) chain A residue 39 type sequence D description binding site for residue EDO A 304 source : AC4 14) chain B residue 0 type sequence M description binding site for residue EDO A 304 source : AC4 15) chain A residue 85 type sequence Y description binding site for residue EDO A 305 source : AC5 16) chain A residue 121 type sequence K description binding site for residue EDO A 305 source : AC5 17) chain A residue 122 type sequence D description binding site for residue EDO A 305 source : AC5 18) chain A residue 137 type sequence D description binding site for residue EDO A 305 source : AC5 19) chain A residue 76 type sequence V description binding site for residue EDO A 306 source : AC6 20) chain A residue 79 type sequence G description binding site for residue EDO A 306 source : AC6 21) chain A residue 80 type sequence T description binding site for residue EDO A 306 source : AC6 22) chain A residue 55 type sequence E description binding site for residue EDO A 307 source : AC7 23) chain A residue 56 type sequence G description binding site for residue EDO A 307 source : AC7 24) chain A residue 57 type sequence P description binding site for residue EDO A 307 source : AC7 25) chain A residue 60 type sequence W description binding site for residue EDO A 307 source : AC7 26) chain A residue 107 type sequence W description binding site for residue EDO A 308 source : AC8 27) chain A residue 173 type sequence E description binding site for residue EDO A 308 source : AC8 28) chain A residue 176 type sequence K description binding site for residue EDO A 308 source : AC8 29) chain A residue 180 type sequence Q description binding site for residue EDO A 308 source : AC8 30) chain A residue 122 type sequence D description binding site for residue EDO A 309 source : AC9 31) chain A residue 13 type sequence S description binding site for residue EDO A 310 source : AD1 32) chain A residue 14 type sequence R description binding site for residue EDO A 310 source : AD1 33) chain A residue 17 type sequence R description binding site for residue EDO A 310 source : AD1 34) chain A residue 92 type sequence S description binding site for residue EDO A 310 source : AD1 35) chain B residue 34 type sequence D description binding site for residue EDO A 310 source : AD1 36) chain A residue 35 type sequence R description binding site for residue GOL A 311 source : AD2 37) chain A residue 40 type sequence A description binding site for residue GOL A 311 source : AD2 38) chain A residue 41 type sequence A description binding site for residue GOL A 311 source : AD2 39) chain A residue 88 type sequence S description binding site for residue GOL A 311 source : AD2 40) chain A residue 87 type sequence Q description binding site for residue GOL A 312 source : AD3 41) chain A residue 88 type sequence S description binding site for residue GOL A 312 source : AD3 42) chain A residue 93 type sequence H description binding site for residue GOL A 312 source : AD3 43) chain A residue 16 type sequence G description binding site for residue GOL A 313 source : AD4 44) chain A residue 17 type sequence R description binding site for residue GOL A 313 source : AD4 45) chain A residue 18 type sequence G description binding site for residue GOL A 313 source : AD4 46) chain B residue 3 type sequence R description binding site for residue GOL A 313 source : AD4 47) chain A residue 219 type sequence R description binding site for residue SO4 A 314 source : AD5 48) chain A residue 256 type sequence R description binding site for residue SO4 A 314 source : AD5 49) chain B residue 19 type sequence K description binding site for residue SO4 A 314 source : AD5 50) chain B residue 20 type sequence S description binding site for residue SO4 A 314 source : AD5 51) chain A residue 21 type sequence R description binding site for residue SO4 A 315 source : AD6 52) chain A residue 98 type sequence M description binding site for residue EDO B 301 source : AD7 53) chain A residue 115 type sequence Q description binding site for residue EDO B 301 source : AD7 54) chain B residue 57 type sequence S description binding site for residue EDO B 301 source : AD7 55) chain B residue 58 type sequence K description binding site for residue EDO B 301 source : AD7 56) chain B residue 60 type sequence W description binding site for residue EDO B 301 source : AD7 57) chain A residue 206 type sequence L description binding site for residue EDO B 302 source : AD8 58) chain A residue 234 type sequence R description binding site for residue EDO B 302 source : AD8 59) chain A residue 242 type sequence Q description binding site for residue EDO B 302 source : AD8 60) chain B residue 10 type sequence Y description binding site for residue EDO B 302 source : AD8 61) chain B residue 11 type sequence S description binding site for residue EDO B 302 source : AD8 62) chain B residue 13 type sequence H description binding site for residue EDO B 302 source : AD8 63) chain B residue 14 type sequence P description binding site for residue EDO B 302 source : AD8 64) chain A residue 234 type sequence R description binding site for residue EDO B 303 source : AD9 65) chain B residue 8 type sequence Q description binding site for residue EDO B 303 source : AD9 66) chain B residue 9 type sequence V description binding site for residue EDO B 303 source : AD9 67) chain B residue 99 type sequence M description binding site for residue EDO B 303 source : AD9 68) chain B residue 95 type sequence W description binding site for residue EDO B 304 source : AE1 69) chain B residue 96 type sequence D description binding site for residue EDO B 304 source : AE1 70) chain B residue 6 type sequence K description binding site for residue EDO B 305 source : AE2 71) chain B residue 7 type sequence I description binding site for residue EDO B 305 source : AE2 72) chain A residue 138 type sequence M description binding site for residue GOL B 306 source : AE3 73) chain B residue 36 type sequence E description binding site for residue GOL B 306 source : AE3 74) chain B residue 37 type sequence V description binding site for residue GOL B 306 source : AE3 75) chain B residue 38 type sequence D description binding site for residue GOL B 306 source : AE3 76) chain B residue 81 type sequence R description binding site for residue GOL B 306 source : AE3 77) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 78) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 79) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 80) chain B residue 2 type MOD_RES sequence Q description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 81) chain A residue 73 type MOD_RES sequence T description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 82) chain A residue 84 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 83) chain A residue 143 type MOD_RES sequence T description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 84) chain A residue 146 type MOD_RES sequence K description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 85) chain A residue 171 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 86) chain B residue 1 type CARBOHYD sequence I description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 87) chain A residue 159 type CARBOHYD sequence Y description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 88) chain B residue 19 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 90) chain B residue 48 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 91) chain B residue 58 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 92) chain B residue 91 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 93) chain B residue 94 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3

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