eF-site ID 5mep-ABCDEF PDB Code 5mep Chain A, B, C, D, E, F click to enlarge Title Human Leukocyte Antigen A02 presenting ILGKFLHWL Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5MEP) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  ILGKFLHWL D:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP E:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM F:  ILGKFLHWL Description Functional site 1) chain A residue 185 type sequence P description binding site for residue EDO A 301 source : AC1 2) chain A residue 187 type sequence T description binding site for residue EDO A 301 source : AC1 3) chain A residue 8 type sequence F description binding site for residue SO4 A 302 source : AC2 4) chain A residue 29 type sequence D description binding site for residue SO4 A 302 source : AC2 5) chain A residue 30 type sequence D description binding site for residue SO4 A 302 source : AC2 6) chain B residue 63 type sequence Y description binding site for residue SO4 A 302 source : AC2 7) chain A residue 234 type sequence R description binding site for residue EDO B 101 source : AC3 8) chain A residue 242 type sequence Q description binding site for residue EDO B 101 source : AC3 9) chain B residue 10 type sequence Y description binding site for residue EDO B 101 source : AC3 10) chain B residue 11 type sequence S description binding site for residue EDO B 101 source : AC3 11) chain B residue 13 type sequence H description binding site for residue EDO B 101 source : AC3 12) chain B residue 14 type sequence P description binding site for residue EDO B 101 source : AC3 13) chain B residue 99 type sequence M description binding site for residue EDO B 101 source : AC3 14) chain B residue 8 type sequence Q description binding site for residue EDO B 102 source : AC4 15) chain B residue 9 type sequence V description binding site for residue EDO B 102 source : AC4 16) chain B residue 94 type sequence K description binding site for residue EDO B 102 source : AC4 17) chain B residue 96 type sequence D description binding site for residue EDO B 102 source : AC4 18) chain B residue 33 type sequence S description binding site for residue EDO B 103 source : AC5 19) chain B residue 34 type sequence D description binding site for residue EDO B 103 source : AC5 20) chain B residue 38 type sequence D description binding site for residue EDO B 104 source : AC6 21) chain B residue 81 type sequence R description binding site for residue EDO B 104 source : AC6 22) chain B residue 83 type sequence N description binding site for residue EDO B 104 source : AC6 23) chain B residue 90 type sequence P description binding site for residue EDO B 104 source : AC6 24) chain B residue 83 type sequence N description binding site for residue EDO B 105 source : AC7 25) chain B residue 84 type sequence H description binding site for residue EDO B 105 source : AC7 26) chain B residue 87 type sequence L description binding site for residue EDO B 105 source : AC7 27) chain D residue 219 type sequence R description binding site for residue EDO B 105 source : AC7 28) chain D residue 222 type sequence E description binding site for residue EDO B 105 source : AC7 29) chain D residue 213 type sequence I description binding site for residue EDO D 301 source : AC8 30) chain D residue 214 type sequence T description binding site for residue EDO D 301 source : AC8 31) chain D residue 263 type sequence H description binding site for residue EDO D 301 source : AC8 32) chain D residue 75 type sequence R description binding site for residue EDO D 302 source : AC9 33) chain D residue 78 type sequence L description binding site for residue EDO D 302 source : AC9 34) chain D residue 82 type sequence R description binding site for residue EDO D 302 source : AC9 35) chain A residue 177 type sequence E description binding site for residue EDO D 303 source : AD1 36) chain D residue 169 type sequence R description binding site for residue EDO D 303 source : AD1 37) chain D residue 173 type sequence E description binding site for residue EDO D 303 source : AD1 38) chain D residue 92 type sequence S description binding site for residue EDO D 304 source : AD2 39) chain E residue 32 type sequence P description binding site for residue EDO D 304 source : AD2 40) chain E residue 34 type sequence D description binding site for residue EDO D 304 source : AD2 41) chain D residue 21 type sequence R description binding site for residue EDO E 101 source : AD3 42) chain E residue 34 type sequence D description binding site for residue EDO E 101 source : AD3 43) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 44) chain D residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 45) 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 46) chain E residue 58 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 47) chain E residue 91 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 48) chain E residue 94 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 49) 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 50) 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 51) 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 52) 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 53) 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 54) chain E residue 19 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 55) chain E residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 56) chain E residue 48 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 57) 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 58) chain D 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 59) chain D 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 60) chain D 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 61) chain E 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 62) 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 63) 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 64) 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 65) 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 66) chain D residue 7 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 67) chain D 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 68) chain D 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 69) 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 70) chain E 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 71) chain D residue 116 type CARBOHYD sequence Y description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 72) chain D 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 73) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 74) 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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