eF-site ID 5c0g-ABC PDB Code 5c0g Chain A, B, C click to enlarge Title HLA-A02 carrying YLGGPDFPTI Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5C0G) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  YLGGPDFPTI Description Functional site 1) chain A residue 19 type sequence E description binding site for residue EDO A 301 source : AC1 2) chain A residue 20 type sequence P description binding site for residue EDO A 301 source : AC1 3) chain A residue 71 type sequence S description binding site for residue EDO A 301 source : AC1 4) chain A residue 75 type sequence R description binding site for residue EDO A 301 source : AC1 5) chain A residue 105 type sequence S description binding site for residue EDO A 302 source : AC2 6) chain A residue 107 type sequence W description binding site for residue EDO A 302 source : AC2 7) chain A residue 195 type sequence S description binding site for residue EDO A 302 source : AC2 8) chain A residue 197 type sequence H description binding site for residue EDO A 302 source : AC2 9) chain A residue 198 type sequence E description binding site for residue EDO A 302 source : AC2 10) chain A residue 6 type sequence R description binding site for residue EDO A 303 source : AC3 11) chain A residue 8 type sequence F description binding site for residue EDO A 303 source : AC3 12) chain A residue 29 type sequence D description binding site for residue EDO A 303 source : AC3 13) chain A residue 18 type sequence G description binding site for residue EDO A 304 source : AC4 14) chain A residue 19 type sequence E description binding site for residue EDO A 304 source : AC4 15) chain A residue 104 type sequence G description binding site for residue EDO A 305 source : AC5 16) chain A residue 106 type sequence D description binding site for residue EDO A 305 source : AC5 17) chain A residue 108 type sequence R description binding site for residue EDO A 305 source : AC5 18) chain A residue 109 type sequence F description binding site for residue EDO A 305 source : AC5 19) chain A residue 6 type sequence R description binding site for residue EDO A 306 source : AC6 20) chain A residue 8 type sequence F description binding site for residue EDO A 306 source : AC6 21) chain B residue 58 type sequence K description binding site for residue EDO A 306 source : AC6 22) chain A residue 170 type sequence R description binding site for residue EDO A 307 source : AC7 23) chain A residue 91 type sequence G description binding site for residue EDO A 308 source : AC8 24) chain A residue 92 type sequence S description binding site for residue EDO A 308 source : AC8 25) chain A residue 2 type sequence S description binding site for residue EDO A 309 source : AC9 26) chain A residue 3 type sequence H description binding site for residue EDO A 309 source : AC9 27) chain A residue 102 type sequence D description binding site for residue EDO A 309 source : AC9 28) chain A residue 14 type sequence R description binding site for residue EDO A 310 source : AD1 29) chain A residue 21 type sequence R description binding site for residue EDO A 310 source : AD1 30) chain A residue 39 type sequence D description binding site for residue EDO A 310 source : AD1 31) chain A residue 14 type sequence R description binding site for residue SO4 A 311 source : AD2 32) chain A residue 15 type sequence P description binding site for residue SO4 A 311 source : AD2 33) chain A residue 16 type sequence G description binding site for residue SO4 A 311 source : AD2 34) chain A residue 17 type sequence R description binding site for residue SO4 A 311 source : AD2 35) chain A residue 206 type sequence L description binding site for residue EDO B 101 source : AD3 36) chain A residue 234 type sequence R description binding site for residue EDO B 101 source : AD3 37) chain A residue 242 type sequence Q description binding site for residue EDO B 101 source : AD3 38) chain B residue 11 type sequence S description binding site for residue EDO B 101 source : AD3 39) chain B residue 13 type sequence H description binding site for residue EDO B 101 source : AD3 40) chain B residue 14 type sequence P description binding site for residue EDO B 101 source : AD3 41) chain A residue 115 type sequence Q description binding site for residue EDO B 102 source : AD4 42) chain B residue 56 type sequence F description binding site for residue EDO B 102 source : AD4 43) chain B residue 57 type sequence S description binding site for residue EDO B 102 source : AD4 44) chain B residue 58 type sequence K description binding site for residue EDO B 102 source : AD4 45) chain B residue 60 type sequence W description binding site for residue EDO B 102 source : AD4 46) chain A residue 21 type sequence R description binding site for residue EDO B 103 source : AD5 47) chain B residue 33 type sequence S description binding site for residue EDO B 103 source : AD5 48) chain B residue 34 type sequence D description binding site for residue EDO B 103 source : AD5 49) chain A residue 235 type sequence P description binding site for residue EDO B 104 source : AD6 50) chain B residue 52 type sequence S description binding site for residue EDO B 104 source : AD6 51) chain B residue 63 type sequence Y description binding site for residue EDO B 104 source : AD6 52) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 68) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290

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