eF-site ID 5men-ABCDE PDB Code 5men Chain A, B, C, D, E click to enlarge Title Human Leukocyte Antigen A02 presenting ILAKFLHWL, in complex with cognate T-Cell Receptor Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source null (K7N5M4_HUMAN) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  ILAKFLHWL D:  IQVEQSPPDLILQEGANSTLRCNFSDSVNNLQWFHQNPWG QLINLFYIPSGTKQNGRLSATTVATERYSLLYISSSQTTD SGVYFCAVDSATSGTYKYIFGTGTRLKVLANIQNPDPAVY QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPS E:  AGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGM GLRLIHYSVGAGITDQGEVPNGYNVSRSTTEDFPLRLLSA APSQTSVYFCASSYQGTEAFFGQGTRLTVVEDLNKVFPPE VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGK EVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQDP RNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD Description Functional site 1) chain A residue 14 type sequence R 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 38 type sequence S description binding site for residue EDO A 301 source : AC1 4) chain A residue 39 type sequence D description binding site for residue EDO A 301 source : AC1 5) chain A residue 85 type sequence Y description binding site for residue EDO A 302 source : AC2 6) chain A residue 118 type sequence Y description binding site for residue EDO A 302 source : AC2 7) chain A residue 121 type sequence K description binding site for residue EDO A 302 source : AC2 8) chain A residue 122 type sequence D description binding site for residue EDO A 302 source : AC2 9) chain A residue 137 type sequence D description binding site for residue EDO A 302 source : AC2 10) chain A residue 35 type sequence R description binding site for residue GOL A 303 source : AC3 11) chain A residue 40 type sequence A description binding site for residue GOL A 303 source : AC3 12) chain A residue 41 type sequence A description binding site for residue GOL A 303 source : AC3 13) chain A residue 15 type sequence P description binding site for residue SO4 A 304 source : AC4 14) chain A residue 16 type sequence G description binding site for residue SO4 A 304 source : AC4 15) chain A residue 17 type sequence R description binding site for residue SO4 A 304 source : AC4 16) chain A residue 18 type sequence G description binding site for residue SO4 A 304 source : AC4 17) chain A residue 2 type sequence S description binding site for residue SO4 A 305 source : AC5 18) chain A residue 3 type sequence H description binding site for residue SO4 A 305 source : AC5 19) chain A residue 4 type sequence S description binding site for residue SO4 A 305 source : AC5 20) chain A residue 102 type sequence D description binding site for residue SO4 A 305 source : AC5 21) chain A residue 105 type sequence S description binding site for residue SO4 A 306 source : AC6 22) chain A residue 107 type sequence W description binding site for residue SO4 A 306 source : AC6 23) chain B residue 10 type sequence Y description binding site for residue EDO B 301 source : AC7 24) chain B residue 11 type sequence S description binding site for residue EDO B 301 source : AC7 25) chain B residue 12 type sequence R description binding site for residue EDO B 301 source : AC7 26) chain B residue 13 type sequence H description binding site for residue EDO B 301 source : AC7 27) chain B residue 14 type sequence P description binding site for residue EDO B 301 source : AC7 28) chain A residue 98 type sequence M description binding site for residue EDO B 302 source : AC8 29) chain A residue 115 type sequence Q description binding site for residue EDO B 302 source : AC8 30) chain B residue 57 type sequence S description binding site for residue EDO B 302 source : AC8 31) chain B residue 58 type sequence K description binding site for residue EDO B 302 source : AC8 32) chain B residue 60 type sequence W description binding site for residue EDO B 302 source : AC8 33) chain B residue 8 type sequence Q description binding site for residue EDO B 303 source : AC9 34) chain B residue 9 type sequence V description binding site for residue EDO B 303 source : AC9 35) chain B residue 94 type sequence K description binding site for residue EDO B 303 source : AC9 36) chain B residue 96 type sequence D description binding site for residue EDO B 303 source : AC9 37) chain A residue 219 type sequence R description binding site for residue SO4 B 304 source : AD1 38) chain A residue 256 type sequence R description binding site for residue SO4 B 304 source : AD1 39) chain B residue 19 type sequence K description binding site for residue SO4 B 304 source : AD1 40) chain B residue 20 type sequence S description binding site for residue SO4 B 304 source : AD1 41) chain D residue 164 type sequence R description binding site for residue SO4 E 301 source : AD2 42) chain E residue 163 type sequence V description binding site for residue SO4 E 301 source : AD2 43) chain E residue 164 type sequence H description binding site for residue SO4 E 301 source : AD2 44) chain E residue 165 type sequence S description binding site for residue SO4 E 301 source : AD2 45) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 46) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 47) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 48) chain D residue 24 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 84 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 143 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 146 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 171 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 53) chain E residue 65 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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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