eF-site ID 5nmf-F PDB Code 5nmf Chain F click to enlarge Title 868 TCR in complex with HLA A02 presenting SLYNTIATL Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5NMF) Sequence F:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP Description Functional site 1) chain F residue 21 type sequence R description binding site for residue EDO F 301 source : AD7 2) chain F residue 35 type sequence R description binding site for residue EDO F 302 source : AD8 3) chain F residue 193 type sequence A description binding site for residue EDO F 303 source : AD9 4) chain F residue 166 type sequence E description binding site for residue EDO F 304 source : AE1 5) chain F residue 170 type sequence R description binding site for residue EDO F 304 source : AE1 6) chain F residue 87 type sequence Q description binding site for residue EDO F 305 source : AE2 7) chain F residue 88 type sequence S description binding site for residue EDO F 305 source : AE2 8) chain F residue 127 type sequence K description binding site for residue EDO F 306 source : AE3 9) chain F residue 135 type sequence A description binding site for residue EDO F 306 source : AE3 10) chain F residue 144 type sequence K description binding site for residue EDO F 306 source : AE3 11) chain F residue 86 type sequence N description binding site for residue SO4 F 307 source : AE4 12) chain F residue 131 type sequence R description binding site for residue SO4 F 308 source : AE5 13) chain F residue 151 type sequence H description binding site for residue SO4 F 308 source : AE5 14) chain F residue 153 type sequence A description binding site for residue SO4 F 308 source : AE5 15) chain F residue 154 type sequence E description binding site for residue SO4 F 308 source : AE5 16) chain F residue 127 type sequence K description binding site for residue EDO I 301 source : AE6 17) chain F residue 128 type sequence E description binding site for residue EDO I 301 source : AE6 18) chain F residue 82 type sequence R description binding site for residue EDO J 305 source : AF3 19) chain F residue 89 type sequence E description binding site for residue EDO J 305 source : AF3 20) chain F residue 65 type sequence R description binding site for residue EDO J 306 source : AF4 21) chain F residue 72 type sequence Q description binding site for residue EDO J 306 source : AF4 22) chain F 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 23) chain F 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 24) chain F 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 25) chain F 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 26) chain F 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 27) chain F 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 28) chain F 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 29) chain F 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 30) 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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