eF-site ID 5c0i-ABC PDB Code 5c0i Chain A, B, C click to enlarge Title HAL-A02 carrying RQFGPDFPTI Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5C0I) Sequence A:  MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSD AASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLG TLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAY LEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEA TLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  RQFGPDFPTI Description Functional site 1) chain A residue 212 type sequence E description binding site for residue EDO A 301 source : AC1 2) chain A residue 213 type sequence I description binding site for residue EDO A 301 source : AC1 3) chain A residue 214 type sequence T description binding site for residue EDO A 301 source : AC1 4) chain A residue 262 type sequence Q description binding site for residue EDO A 301 source : AC1 5) chain A residue 263 type sequence H description binding site for residue EDO A 301 source : AC1 6) chain A residue 264 type sequence E description binding site for residue EDO A 301 source : AC1 7) chain A residue 105 type sequence S description binding site for residue EDO A 302 source : AC2 8) chain A residue 107 type sequence W description binding site for residue EDO A 302 source : AC2 9) chain A residue 195 type sequence S description binding site for residue EDO A 302 source : AC2 10) chain A residue 198 type sequence E description binding site for residue EDO A 302 source : AC2 11) chain A residue 138 type sequence M description binding site for residue EDO A 303 source : AC3 12) chain A residue 141 type sequence Q description binding site for residue EDO A 303 source : AC3 13) chain A residue 142 type sequence T description binding site for residue EDO A 303 source : AC3 14) chain A residue 14 type sequence R description binding site for residue EDO A 304 source : AC4 15) chain A residue 18 type sequence G description binding site for residue EDO A 304 source : AC4 16) chain A residue 19 type sequence E description binding site for residue EDO A 304 source : AC4 17) chain A residue 44 type sequence R description binding site for residue EDO A 305 source : AC5 18) chain A residue 45 type sequence M description binding site for residue EDO A 305 source : AC5 19) chain A residue 60 type sequence W description binding site for residue EDO A 305 source : AC5 20) chain A residue 6 type sequence R description binding site for residue GOL A 306 source : AC6 21) chain A residue 8 type sequence F description binding site for residue GOL A 306 source : AC6 22) chain A residue 27 type sequence Y description binding site for residue GOL A 306 source : AC6 23) chain A residue 29 type sequence D description binding site for residue GOL A 306 source : AC6 24) chain A residue 30 type sequence D description binding site for residue GOL A 306 source : AC6 25) chain B residue 63 type sequence Y description binding site for residue GOL A 306 source : AC6 26) chain A residue 68 type sequence K description binding site for residue GOL A 307 source : AC7 27) chain A residue 69 type sequence A description binding site for residue GOL A 307 source : AC7 28) chain A residue 72 type sequence Q description binding site for residue GOL A 307 source : AC7 29) chain A residue 166 type sequence E description binding site for residue SO4 A 308 source : AC8 30) chain A residue 167 type sequence W description binding site for residue SO4 A 308 source : AC8 31) chain A residue 170 type sequence R description binding site for residue SO4 A 308 source : AC8 32) chain A residue 128 type sequence E description binding site for residue SO4 A 309 source : AC9 33) chain A residue 129 type sequence D description binding site for residue SO4 A 309 source : AC9 34) chain A residue 130 type sequence L description binding site for residue SO4 A 309 source : AC9 35) chain A residue 131 type sequence R description binding site for residue SO4 A 309 source : AC9 36) chain A residue 157 type sequence R description binding site for residue SO4 A 309 source : AC9 37) chain A residue 161 type sequence E description binding site for residue SO4 A 309 source : AC9 38) chain B residue 83 type sequence N description binding site for residue CA B 101 source : AD1 39) chain B residue 84 type sequence H description binding site for residue CA B 101 source : AD1 40) chain B residue 87 type sequence L description binding site for residue CA B 101 source : AD1 41) chain A residue 206 type sequence L description binding site for residue EDO B 102 source : AD2 42) chain A residue 234 type sequence R description binding site for residue EDO B 102 source : AD2 43) chain A residue 242 type sequence Q description binding site for residue EDO B 102 source : AD2 44) chain B residue 10 type sequence Y description binding site for residue EDO B 102 source : AD2 45) chain B residue 11 type sequence S description binding site for residue EDO B 102 source : AD2 46) chain B residue 13 type sequence H description binding site for residue EDO B 102 source : AD2 47) chain B residue 14 type sequence P description binding site for residue EDO B 102 source : AD2 48) chain A residue 21 type sequence R description binding site for residue EDO B 103 source : AD3 49) chain B residue 33 type sequence S description binding site for residue EDO B 103 source : AD3 50) chain B residue 34 type sequence D description binding site for residue EDO B 103 source : AD3 51) chain B residue 95 type sequence W description binding site for residue EDO B 104 source : AD4 52) chain B residue 97 type sequence R description binding site for residue EDO B 104 source : AD4 53) chain A residue 115 type sequence Q description binding site for residue EDO B 105 source : AD5 54) chain B residue 57 type sequence S description binding site for residue EDO B 105 source : AD5 55) chain B residue 58 type sequence K description binding site for residue EDO B 105 source : AD5 56) chain B residue 60 type sequence W description binding site for residue EDO B 105 source : AD5 57) chain A residue 235 type sequence P description binding site for residue EDO B 106 source : AD6 58) chain B residue 52 type sequence S description binding site for residue EDO B 106 source : AD6 59) chain B residue 63 type sequence Y description binding site for residue EDO B 106 source : AD6 60) chain B residue 8 type sequence Q description binding site for residue GOL B 107 source : AD7 61) chain B residue 9 type sequence V description binding site for residue GOL B 107 source : AD7 62) chain B residue 94 type sequence K description binding site for residue GOL B 107 source : AD7 63) chain B residue 96 type sequence D description binding site for residue GOL B 107 source : AD7 64) chain A residue 23 type sequence I description binding site for residue GOL B 108 source : AD8 65) chain A residue 37 type sequence D description binding site for residue GOL B 108 source : AD8 66) chain B residue 51 type sequence H description binding site for residue GOL B 108 source : AD8 67) chain B residue 52 type sequence S description binding site for residue GOL B 108 source : AD8 68) chain B residue 53 type sequence D description binding site for residue GOL B 108 source : AD8 69) chain B residue 54 type sequence L description binding site for residue GOL B 108 source : AD8 70) chain B residue 64 type sequence L description binding site for residue GOL B 108 source : AD8 71) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 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 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 87) 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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