eF-site ID 4u1l-ABCDEF PDB Code 4u1l Chain A, B, C, D, E, F click to enlarge Title HLA class I micropolymorphisms determine peptide-HLA landscape and dictate differential HIV-1 escape through identical epitopes Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, B-81 alpha chain Source Homo sapiens (Human) (Q90VG9_9HIV1) Sequence A:  MGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSD AASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLR NLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYD GKDYIALNEDLRSWTAADTAAQISQRKLEAARVAEQLRAY LEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEA TLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDR TFQKWTAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  RPQVPLRPM D:  MGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSD AASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLR NLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYD GKDYIALNEDLRSWTAADTAAQISQRKLEAARVAEQLRAY LEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEA TLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDR TFQKWTAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP E:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM F:  RPQVPLRPM Description Functional site 1) chain A residue 44 type sequence R description binding site for residue GOL A 301 source : AC1 2) chain A residue 45 type sequence E description binding site for residue GOL A 301 source : AC1 3) chain A residue 57 type sequence P description binding site for residue GOL A 301 source : AC1 4) chain A residue 60 type sequence W description binding site for residue GOL A 301 source : AC1 5) chain A residue 61 type sequence D description binding site for residue GOL A 301 source : AC1 6) chain A residue 64 type sequence T description binding site for residue GOL A 301 source : AC1 7) chain D residue 72 type sequence Q description binding site for residue GOL A 301 source : AC1 8) chain D residue 75 type sequence R description binding site for residue GOL A 301 source : AC1 9) chain A residue 80 type sequence N description binding site for residue GOL A 302 source : AC2 10) chain A residue 83 type sequence G description binding site for residue GOL A 302 source : AC2 11) chain A residue 84 type sequence Y description binding site for residue GOL A 302 source : AC2 12) chain A residue 146 type sequence K description binding site for residue GOL A 302 source : AC2 13) chain D residue 154 type sequence E description binding site for residue GOL A 302 source : AC2 14) chain D residue 157 type sequence R description binding site for residue GOL A 302 source : AC2 15) chain D residue 158 type sequence A description binding site for residue GOL A 302 source : AC2 16) chain D residue 161 type sequence E description binding site for residue GOL A 302 source : AC2 17) chain A residue 70 type sequence Q description binding site for residue EDO A 303 source : AC3 18) chain A residue 97 type sequence S description binding site for residue EDO A 303 source : AC3 19) chain A residue 99 type sequence Y description binding site for residue EDO A 303 source : AC3 20) chain A residue 114 type sequence N description binding site for residue EDO A 303 source : AC3 21) chain A residue 116 type sequence Y description binding site for residue EDO A 303 source : AC3 22) chain C residue 3 type sequence Q description binding site for residue EDO A 303 source : AC3 23) chain A residue 62 type sequence R description binding site for residue EDO A 304 source : AC4 24) chain A residue 65 type sequence Q description binding site for residue EDO A 304 source : AC4 25) chain A residue 62 type sequence R description binding site for residue EDO A 305 source : AC5 26) chain D residue 144 type sequence Q description binding site for residue EDO A 305 source : AC5 27) chain D residue 145 type sequence R description binding site for residue EDO A 305 source : AC5 28) chain D residue 148 type sequence E description binding site for residue EDO A 305 source : AC5 29) chain A residue 73 type sequence T description binding site for residue EDO A 306 source : AC6 30) chain A residue 74 type sequence D description binding site for residue EDO A 306 source : AC6 31) chain A residue 77 type sequence S description binding site for residue EDO A 306 source : AC6 32) chain C residue 7 type sequence R description binding site for residue EDO A 306 source : AC6 33) chain A residue 115 type sequence Q description binding site for residue EDO A 307 source : AC7 34) chain A residue 116 type sequence Y description binding site for residue EDO A 307 source : AC7 35) chain A residue 122 type sequence D description binding site for residue EDO A 307 source : AC7 36) chain A residue 124 type sequence I description binding site for residue EDO A 307 source : AC7 37) chain A residue 125 type sequence A description binding site for residue EDO A 307 source : AC7 38) chain A residue 134 type sequence T description binding site for residue EDO A 307 source : AC7 39) chain B residue 60 type sequence W description binding site for residue EDO A 307 source : AC7 40) chain A residue 150 type sequence A description binding site for residue SO4 A 308 source : AC8 41) chain A residue 151 type sequence R description binding site for residue SO4 A 308 source : AC8 42) chain D residue 83 type sequence G description binding site for residue SO4 A 308 source : AC8 43) chain D residue 84 type sequence Y description binding site for residue SO4 A 308 source : AC8 44) chain D residue 85 type sequence Y description binding site for residue SO4 A 308 source : AC8 45) chain D residue 86 type sequence N description binding site for residue SO4 A 308 source : AC8 46) chain A residue 8 type sequence F description binding site for residue SO4 A 309 source : AC9 47) chain A residue 27 type sequence Y description binding site for residue SO4 A 309 source : AC9 48) chain A residue 29 type sequence D description binding site for residue SO4 A 309 source : AC9 49) chain A residue 30 type sequence D description binding site for residue SO4 A 309 source : AC9 50) chain A residue 8 type sequence F description binding site for residue EDO B 101 source : AD1 51) chain A residue 98 type sequence M description binding site for residue EDO B 101 source : AD1 52) chain A residue 115 type sequence Q description binding site for residue EDO B 101 source : AD1 53) chain B residue 57 type sequence S description binding site for residue EDO B 101 source : AD1 54) chain B residue 58 type sequence K description binding site for residue EDO B 101 source : AD1 55) chain A residue 57 type sequence P description binding site for residue GOL D 301 source : AD2 56) chain D residue 38 type sequence S description binding site for residue GOL D 301 source : AD2 57) chain D residue 68 type sequence K description binding site for residue GOL D 301 source : AD2 58) chain D residue 71 type sequence A description binding site for residue GOL D 301 source : AD2 59) chain D residue 72 type sequence Q description binding site for residue GOL D 301 source : AD2 60) chain D residue 75 type sequence R description binding site for residue GOL D 301 source : AD2 61) chain D residue 62 type sequence R description binding site for residue EDO D 302 source : AD3 62) chain D residue 65 type sequence Q description binding site for residue EDO D 302 source : AD3 63) chain D residue 70 type sequence Q description binding site for residue EDO D 303 source : AD4 64) chain D residue 99 type sequence Y description binding site for residue EDO D 303 source : AD4 65) chain D residue 114 type sequence N description binding site for residue EDO D 303 source : AD4 66) chain D residue 116 type sequence Y description binding site for residue EDO D 303 source : AD4 67) chain F residue 3 type sequence Q description binding site for residue EDO D 303 source : AD4 68) chain A residue 61 type sequence D description binding site for residue EDO D 304 source : AD5 69) chain D residue 14 type sequence R description binding site for residue EDO D 304 source : AD5 70) chain D residue 20 type sequence P description binding site for residue EDO D 304 source : AD5 71) chain D residue 21 type sequence R description binding site for residue EDO D 304 source : AD5 72) chain D residue 38 type sequence S description binding site for residue EDO D 304 source : AD5 73) chain D residue 39 type sequence D description binding site for residue EDO D 304 source : AD5 74) chain D residue 75 type sequence R description binding site for residue EDO D 304 source : AD5 75) chain D residue 73 type sequence T description binding site for residue EDO D 305 source : AD6 76) chain D residue 74 type sequence D description binding site for residue EDO D 305 source : AD6 77) chain D residue 77 type sequence S description binding site for residue EDO D 305 source : AD6 78) chain D residue 95 type sequence L description binding site for residue EDO D 305 source : AD6 79) chain F residue 7 type sequence R description binding site for residue EDO D 305 source : AD6 80) chain D residue 27 type sequence Y description binding site for residue EDO D 306 source : AD7 81) chain D residue 29 type sequence D description binding site for residue EDO D 306 source : AD7 82) chain D residue 30 type sequence D description binding site for residue EDO D 306 source : AD7 83) chain D residue 122 type sequence D description binding site for residue EDO D 307 source : AD8 84) chain D residue 125 type sequence A description binding site for residue EDO D 307 source : AD8 85) chain D residue 134 type sequence T description binding site for residue EDO D 307 source : AD8 86) chain A residue 68 type sequence K description binding site for residue EDO D 308 source : AD9 87) chain D residue 13 type sequence S description binding site for residue EDO D 308 source : AD9 88) chain D residue 19 type sequence E description binding site for residue EDO D 308 source : AD9 89) chain A residue 83 type sequence G description binding site for residue EDO D 309 source : AE1 90) chain A residue 84 type sequence Y description binding site for residue EDO D 309 source : AE1 91) chain A residue 86 type sequence N description binding site for residue EDO D 309 source : AE1 92) chain D residue 150 type sequence A description binding site for residue EDO D 309 source : AE1 93) chain D residue 151 type sequence R description binding site for residue EDO D 309 source : AE1 94) chain F residue 7 type sequence R description binding site for residue EDO D 309 source : AE1 95) chain D residue 19 type sequence E description binding site for residue EDO D 310 source : AE2 96) chain D residue 20 type sequence P description binding site for residue EDO D 310 source : AE2 97) chain D residue 79 type sequence R description binding site for residue EDO D 310 source : AE2 98) chain D residue 12 type sequence V description binding site for residue EDO E 101 source : AE3 99) chain D residue 92 type sequence S description binding site for residue EDO E 101 source : AE3 100) chain E residue 32 type sequence P description binding site for residue EDO E 101 source : AE3 101) chain E residue 33 type sequence S description binding site for residue EDO E 101 source : AE3 102) chain E residue 34 type sequence D description binding site for residue EDO E 101 source : AE3 103) chain D residue 21 type sequence R description binding site for residue EDO E 102 source : AE4 104) chain E residue 33 type sequence S description binding site for residue EDO E 102 source : AE4 105) chain E residue 34 type sequence D description binding site for residue EDO E 102 source : AE4 106) chain D residue 55 type sequence E description binding site for residue EDO F 101 source : AE5 107) chain D residue 58 type sequence E description binding site for residue EDO F 101 source : AE5 108) chain D residue 59 type sequence Y description binding site for residue EDO F 101 source : AE5 109) chain F residue 1 type sequence R description binding site for residue EDO F 101 source : AE5 110) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 111) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 112) 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 113) chain D residue 143 type MOD_RES sequence S description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 114) 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 115) chain D residue 152 type MOD_RES sequence V description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 116) chain D residue 159 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 117) 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 118) 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 119) chain A residue 143 type MOD_RES sequence S description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 120) 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 121) chain A residue 152 type MOD_RES sequence V description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 122) chain A residue 159 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 123) 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 124) chain D residue 63 type MOD_RES sequence N description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) 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 138) 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 139) 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

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