eF-site ID 2bck-ABCDEF PDB Code 2bck Chain A, B, C, D, E, F click to enlarge Title Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-24 alpha chain Source Homo sapiens (Human) (TERT_HUMAN) Sequence A:  GSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDEETGKVKAHSQTDRENLRI ALRYYNQSEAGSHTLQMMFGCDVGSDGRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQITKRKWEAAHVAEQQRAYL EGTCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEAT LRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPGSGG GLNDIF B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  VYGFVRACL D:  GSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDEETGKVKAHSQTDRENLRI ALRYYNQSEAGSHTLQMMFGCDVGSDGRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQITKRKWEAAHVAEQQRAYL EGTCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEAT LRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPGSGG GLNDIF E:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM F:  VYGFVRACL Description Functional site 1) chain A residue 79 type sequence R description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 2) chain A residue 83 type sequence R description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 3) chain D residue 79 type sequence R description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 4) chain D residue 83 type sequence R description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 5) chain B residue 45 type sequence R description BINDING SITE FOR RESIDUE SO4 B 302 source : AC2 6) chain B residue 47 type sequence E description BINDING SITE FOR RESIDUE SO4 B 302 source : AC2 7) chain D residue 225 type sequence T description BINDING SITE FOR RESIDUE SO4 B 302 source : AC2 8) chain A residue 21 type sequence R description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 9) chain B residue 51 type sequence H description BINDING SITE FOR RESIDUE SO4 B 303 source : AC3 10) chain E residue 45 type sequence R description BINDING SITE FOR RESIDUE SO4 E 304 source : AC4 11) chain E residue 47 type sequence E description BINDING SITE FOR RESIDUE SO4 E 304 source : AC4 12) chain E residue 48 type sequence K description BINDING SITE FOR RESIDUE SO4 E 304 source : AC4 13) chain D residue 21 type sequence R description BINDING SITE FOR RESIDUE SO4 E 305 source : AC5 14) chain E residue 51 type sequence H description BINDING SITE FOR RESIDUE SO4 E 305 source : AC5 15) chain B residue 0 type sequence M description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 16) chain D residue 276 type sequence P description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 17) chain D residue 277 type sequence G description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 18) chain D residue 278 type sequence S description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 19) chain D residue 279 type sequence G description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 20) chain D residue 280 type sequence G description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 21) chain D residue 281 type sequence G description BINDING SITE FOR RESIDUE SO4 D 306 source : AC6 22) chain A residue 275 type sequence E description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 23) chain A residue 276 type sequence P description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 24) chain A residue 277 type sequence G description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 25) chain A residue 278 type sequence S description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 26) chain A residue 279 type sequence G description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 27) chain A residue 280 type sequence G description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 28) chain A residue 281 type sequence G description BINDING SITE FOR RESIDUE SO4 A 307 source : AC7 29) chain A residue 147 type sequence W description BINDING SITE FOR RESIDUE SO4 A 308 source : AC8 30) chain A residue 150 type sequence A description BINDING SITE FOR RESIDUE SO4 A 308 source : AC8 31) chain C residue 8 type sequence C description BINDING SITE FOR RESIDUE SO4 A 308 source : AC8 32) chain D residue 86 type sequence N description BINDING SITE FOR RESIDUE SO4 A 308 source : AC8 33) chain A residue 8 type sequence F description BINDING SITE FOR RESIDUE GOL A 309 source : AC9 34) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE GOL A 309 source : AC9 35) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE GOL A 309 source : AC9 36) chain B residue 56 type sequence F description BINDING SITE FOR RESIDUE GOL A 309 source : AC9 37) chain B residue 63 type sequence Y description BINDING SITE FOR RESIDUE GOL A 309 source : AC9 38) chain D residue 27 type sequence Y description BINDING SITE FOR RESIDUE GOL D 307 source : BC1 39) chain E residue 56 type sequence F description BINDING SITE FOR RESIDUE GOL D 307 source : BC1 40) chain E residue 63 type sequence Y description BINDING SITE FOR RESIDUE GOL D 307 source : BC1 41) chain D residue 204 type sequence W description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 42) chain D residue 234 type sequence R description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 43) chain E residue 11 type sequence S description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 44) chain E residue 12 type sequence R description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 45) chain E residue 13 type sequence H description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 46) chain E residue 14 type sequence P description BINDING SITE FOR RESIDUE GOL E 203 source : BC2 47) chain A residue 204 type sequence W description BINDING SITE FOR RESIDUE GOL B 204 source : BC3 48) chain A residue 242 type sequence Q description BINDING SITE FOR RESIDUE GOL B 204 source : BC3 49) chain B residue 10 type sequence Y description BINDING SITE FOR RESIDUE GOL B 204 source : BC3 50) chain B residue 11 type sequence S description BINDING SITE FOR RESIDUE GOL B 204 source : BC3 51) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH source prosite : PS00290 52) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH source prosite : PS00290 53) 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 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 82) chain D 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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