eF-site ID 6ggm-ABCDPQ PDB Code 6ggm Chain A, B, C, D, P, Q click to enlarge Title HLA-E*01:03 in complex with the Mtb44 peptide variant: Mtb44*P2-Phe. Classification IMMUNE SYSTEM Compound MHC class I antigen Source (6GGM) Sequence A:  GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDA ASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRT LRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDG KDYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYL EDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEAT LRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGT FQKWAAVVVPSGEEQRYTCHVQHEGLPEPVTLRW B:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM C:  GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDA ASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRT LRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDG KDYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYL EDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEAT LRCWALGFYPAEITLTWQQDGQDTELVETRPAGDGTFQKW AAVVVPSGEEQRYTCHVQHEGLPEPVTLRW D:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM P:  RFPAKAPLL Q:  RFPAKAPLL Description Functional site 1) chain A residue 181 type sequence H description binding site for residue ZN A 301 source : AC1 2) chain A residue 183 type sequence E description binding site for residue ZN A 301 source : AC1 3) chain C residue 181 type sequence H description binding site for residue ZN A 301 source : AC1 4) chain C residue 183 type sequence E description binding site for residue ZN A 301 source : AC1 5) chain A residue 152 type sequence E description binding site for residue ZN A 302 source : AC2 6) chain A residue 155 type sequence H description binding site for residue ZN A 302 source : AC2 7) chain C residue 155 type sequence H description binding site for residue ZN A 302 source : AC2 8) chain P residue 5 type sequence K description binding site for residue ZN A 302 source : AC2 9) chain A residue 196 type sequence D description binding site for residue ZN A 303 source : AC3 10) chain A residue 197 type sequence H description binding site for residue ZN A 303 source : AC3 11) chain C residue 196 type sequence D description binding site for residue ZN A 303 source : AC3 12) chain C residue 197 type sequence H description binding site for residue ZN A 303 source : AC3 13) chain A residue 62 type sequence R description binding site for residue SO4 A 304 source : AC4 14) chain A residue 167 type sequence W description binding site for residue SO4 A 304 source : AC4 15) chain P residue 1 type sequence R description binding site for residue SO4 A 304 source : AC4 16) chain A residue 75 type sequence R description binding site for residue SO4 A 305 source : AC5 17) chain A residue 79 type sequence R description binding site for residue SO4 A 305 source : AC5 18) chain A residue 82 type sequence R description binding site for residue SO4 A 305 source : AC5 19) chain B residue 42 type sequence K description binding site for residue SO4 B 201 source : AC6 20) chain B residue 71 type sequence F description binding site for residue SO4 B 201 source : AC6 21) chain B residue 72 type sequence T description binding site for residue SO4 B 201 source : AC6 22) chain B residue 79 type sequence Y description binding site for residue SO4 B 201 source : AC6 23) chain A residue 196 type sequence D description binding site for residue ZN C 301 source : AC7 24) chain A residue 197 type sequence H description binding site for residue ZN C 301 source : AC7 25) chain C residue 196 type sequence D description binding site for residue ZN C 301 source : AC7 26) chain C residue 197 type sequence H description binding site for residue ZN C 301 source : AC7 27) chain D residue 42 type sequence K description binding site for residue SO4 D 201 source : AC8 28) chain D residue 71 type sequence F description binding site for residue SO4 D 201 source : AC8 29) chain D residue 72 type sequence T description binding site for residue SO4 D 201 source : AC8 30) chain D residue 79 type sequence Y description binding site for residue SO4 D 201 source : AC8 31) chain B residue 13 type sequence R description binding site for residue SO4 D 202 source : AC9 32) chain B residue 14 type sequence H description binding site for residue SO4 D 202 source : AC9 33) chain B residue 23 type sequence F description binding site for residue SO4 D 202 source : AC9 34) chain D residue 13 type sequence R description binding site for residue SO4 D 202 source : AC9 35) chain D residue 14 type sequence H description binding site for residue SO4 D 202 source : AC9 36) chain D residue 23 type sequence F description binding site for residue SO4 D 202 source : AC9 37) chain C residue 21 type sequence R description binding site for residue SO4 D 203 source : AD1 38) chain D residue 52 type sequence H description binding site for residue SO4 D 203 source : AD1 39) chain A residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 84 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 146 type BINDING sequence K description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 43) chain A residue 156 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 159 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 46) chain C residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 47) chain C residue 84 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 48) chain C residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 49) chain C residue 146 type BINDING sequence K description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 50) chain C residue 156 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 51) chain C residue 159 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 52) chain C residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18339401 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI5 54) chain C residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 source Swiss-Prot : SWS_FT_FI5 55) chain B residue 79-85 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 56) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 57) chain B residue 3 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 3 type MOD_RES sequence Q description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 2 type CARBOHYD sequence I description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 60) chain D residue 2 type CARBOHYD sequence I description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 61) chain B residue 20 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 42 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 49 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 64) chain B residue 59 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 65) chain B residue 92 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 95 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 67) chain D residue 20 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 68) chain D residue 42 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 69) chain D residue 49 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 70) chain D residue 59 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 92 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 95 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links