eF-site ID 2w72-ABCD PDB Code 2w72 Chain A, B, C, D click to enlarge Title DEOXYGENATED STRUCTURE OF A DISTAL SITE HEMOGLOBIN MUTANT PLUS XE Classification OXYGEN TRANSPORT Compound HUMAN HEMOGLOBIN A Source (HBA_HUMAN) Sequence A:  VLSPADKTNVKAAWGKVGAHAGEYGAEAYERMFLSFPTTK TYFPHFDLSHGSAQVKGQGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR B:  MHLTPEEKSAVTALWGKVNVDEVGGEAYGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAQGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAHKYH C:  MLSPADKTNVKAAWGKVGAHAGEYGAEAYERMFLSFPTTK TYFPHFDLSHGSAQVKGQGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR D:  MHLTPEEKSAVTALWGKVNVDEVGGEAYGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAQGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAHKYH Description Functional site 1) chain A residue 29 type sequence Y description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 2) chain A residue 42 type sequence Y description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 3) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 4) chain A residue 45 type sequence H description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 5) chain A residue 46 type sequence F description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 6) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 7) chain A residue 61 type sequence K description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 8) chain A residue 62 type sequence V description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 9) chain A residue 83 type sequence L description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 10) chain A residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 11) chain A residue 87 type sequence H description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 12) chain A residue 91 type sequence L description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 13) chain A residue 93 type sequence V description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 14) chain A residue 97 type sequence N description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 15) chain A residue 98 type sequence F description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 16) chain A residue 101 type sequence L description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 17) chain A residue 136 type sequence L description BINDING SITE FOR RESIDUE HEM A 1142 source : AC1 18) chain B residue 28 type sequence Y description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 19) chain B residue 41 type sequence F description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 20) chain B residue 63 type sequence Q description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 21) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 22) chain B residue 67 type sequence V description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 23) chain B residue 92 type sequence H description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 24) chain B residue 96 type sequence L description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 25) chain B residue 102 type sequence N description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 26) chain B residue 103 type sequence F description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 27) chain B residue 141 type sequence L description BINDING SITE FOR RESIDUE HEM B 1147 source : AC2 28) chain A residue 45 type sequence H description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 29) chain C residue 29 type sequence Y description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 30) chain C residue 42 type sequence Y description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 31) chain C residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 32) chain C residue 45 type sequence H description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 33) chain C residue 46 type sequence F description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 34) chain C residue 58 type sequence Q description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 35) chain C residue 61 type sequence K description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 36) chain C residue 62 type sequence V description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 37) chain C residue 83 type sequence L description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 38) chain C residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 39) chain C residue 87 type sequence H description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 40) chain C residue 91 type sequence L description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 41) chain C residue 93 type sequence V description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 42) chain C residue 97 type sequence N description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 43) chain C residue 98 type sequence F description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 44) chain C residue 101 type sequence L description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 45) chain C residue 136 type sequence L description BINDING SITE FOR RESIDUE HEM C 1142 source : AC3 46) chain C residue 53 type sequence A description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 47) chain D residue 28 type sequence Y description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 48) chain D residue 41 type sequence F description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 49) chain D residue 63 type sequence Q description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 50) chain D residue 66 type sequence K description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 51) chain D residue 67 type sequence V description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 52) chain D residue 91 type sequence L description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 53) chain D residue 92 type sequence H description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 54) chain D residue 96 type sequence L description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 55) chain D residue 98 type sequence V description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 56) chain D residue 102 type sequence N description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 57) chain D residue 103 type sequence F description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 58) chain D residue 141 type sequence L description BINDING SITE FOR RESIDUE HEM D 1147 source : AC4 59) chain C residue 36 type sequence F description BINDING SITE FOR RESIDUE SO4 C 1143 source : AC5 60) chain C residue 37 type sequence P description BINDING SITE FOR RESIDUE SO4 C 1143 source : AC5 61) chain C residue 38 type sequence T description BINDING SITE FOR RESIDUE SO4 C 1143 source : AC5 62) chain B residue 120 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 63) chain C residue 119 type sequence P description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 64) chain D residue 26 type sequence E description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 65) chain D residue 30 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 66) chain D residue 55 type sequence M description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 67) chain D residue 116 type sequence H description BINDING SITE FOR RESIDUE SO4 D 1148 source : AC6 68) chain B residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 B 1148 source : AC7 69) chain B residue 80 type sequence N description BINDING SITE FOR RESIDUE SO4 B 1148 source : AC7 70) chain B residue 81 type sequence L description BINDING SITE FOR RESIDUE SO4 B 1148 source : AC7 71) chain B residue 82 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1148 source : AC7 72) chain A residue 36 type sequence F description BINDING SITE FOR RESIDUE SO4 A 1143 source : AC8 73) chain A residue 100 type sequence L description BINDING SITE FOR RESIDUE SO4 A 1143 source : AC8 74) chain B residue 116 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1149 source : AC9 75) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1149 source : AC9 76) chain C residue 16 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1149 source : AC9 77) chain A residue 141 type sequence R description BINDING SITE FOR RESIDUE SO4 C 1144 source : BC1 78) chain C residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 C 1144 source : BC1 79) chain C residue 127 type sequence K description BINDING SITE FOR RESIDUE SO4 C 1144 source : BC1 80) chain C residue 130 type sequence A description BINDING SITE FOR RESIDUE SO4 C 1144 source : BC1 81) chain A residue 16 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1144 source : BC2 82) chain A residue 113 type sequence L description BINDING SITE FOR RESIDUE SO4 A 1144 source : BC2 83) chain A residue 114 type sequence P description BINDING SITE FOR RESIDUE SO4 A 1144 source : BC2 84) chain A residue 115 type sequence A description BINDING SITE FOR RESIDUE SO4 A 1144 source : BC2 85) chain A residue 116 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1144 source : BC2 86) chain A residue 5 type sequence A description BINDING SITE FOR RESIDUE SO4 A 1145 source : BC3 87) chain A residue 9 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1145 source : BC3 88) chain B residue 51 type sequence P description BINDING SITE FOR RESIDUE SO4 A 1145 source : BC3 89) chain A residue 127 type sequence K description BINDING SITE FOR RESIDUE PO4 C 1145 source : BC4 90) chain A residue 130 type sequence A description BINDING SITE FOR RESIDUE PO4 C 1145 source : BC4 91) chain C residue 141 type sequence R description BINDING SITE FOR RESIDUE PO4 C 1145 source : BC4 92) chain B residue 62 type sequence A description BINDING SITE FOR RESIDUE K B 1150 source : BC5 93) chain B residue 65 type sequence K description BINDING SITE FOR RESIDUE K B 1150 source : BC5 94) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE K B 1150 source : BC5 95) chain D residue 108 type sequence N description BINDING SITE FOR RESIDUE K C 1146 source : BC6 96) chain A residue 14 type sequence W description BINDING SITE FOR RESIDUE XE A 1146 source : BC8 97) chain A residue 128 type sequence F description BINDING SITE FOR RESIDUE XE A 1146 source : BC8 98) chain A residue 129 type sequence L description BINDING SITE FOR RESIDUE XE A 1146 source : BC8 99) chain A residue 14 type sequence W description BINDING SITE FOR RESIDUE XE A 1147 source : BC9 100) chain A residue 21 type sequence A description BINDING SITE FOR RESIDUE XE A 1147 source : BC9 101) chain A residue 24 type sequence Y description BINDING SITE FOR RESIDUE XE A 1147 source : BC9 102) chain A residue 105 type sequence L description BINDING SITE FOR RESIDUE XE A 1147 source : BC9 103) chain A residue 109 type sequence L description BINDING SITE FOR RESIDUE XE A 1147 source : BC9 104) chain A residue 43 type sequence F description BINDING SITE FOR RESIDUE XE A 1148 source : CC1 105) chain A residue 46 type sequence F description BINDING SITE FOR RESIDUE XE A 1148 source : CC1 106) chain A residue 55 type sequence V description BINDING SITE FOR RESIDUE XE A 1148 source : CC1 107) chain A residue 62 type sequence V description BINDING SITE FOR RESIDUE XE A 1149 source : CC2 108) chain A residue 105 type sequence L description BINDING SITE FOR RESIDUE XE A 1149 source : CC2 109) chain A residue 105 type sequence L description BINDING SITE FOR RESIDUE XE A 1150 source : CC3 110) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE XE A 1151 source : CC4 111) chain A residue 113 type sequence L description BINDING SITE FOR RESIDUE XE A 1151 source : CC4 112) chain A residue 116 type sequence E description BINDING SITE FOR RESIDUE XE A 1151 source : CC4 113) chain C residue 14 type sequence W description BINDING SITE FOR RESIDUE XE C 1147 source : CC5 114) chain C residue 128 type sequence F description BINDING SITE FOR RESIDUE XE C 1147 source : CC5 115) chain C residue 33 type sequence F description BINDING SITE FOR RESIDUE XE C 1148 source : CC6 116) chain C residue 43 type sequence F description BINDING SITE FOR RESIDUE XE C 1148 source : CC6 117) chain C residue 46 type sequence F description BINDING SITE FOR RESIDUE XE C 1148 source : CC6 118) chain C residue 58 type sequence Q description BINDING SITE FOR RESIDUE XE C 1148 source : CC6 119) chain C residue 62 type sequence V description BINDING SITE FOR RESIDUE XE C 1149 source : CC7 120) chain C residue 101 type sequence L description BINDING SITE FOR RESIDUE XE C 1149 source : CC7 121) chain C residue 101 type sequence L description BINDING SITE FOR RESIDUE XE C 1150 source : CC8 122) chain C residue 116 type sequence E description BINDING SITE FOR RESIDUE XE C 1151 source : CC9 123) chain B residue 71 type sequence F description BINDING SITE FOR RESIDUE XE B 1151 source : DC1 124) chain B residue 103 type sequence F description BINDING SITE FOR RESIDUE XE B 1151 source : DC1 125) chain B residue 106 type sequence L description BINDING SITE FOR RESIDUE XE B 1151 source : DC1 126) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE XE B 1151 source : DC1 127) chain B residue 134 type sequence V description BINDING SITE FOR RESIDUE XE B 1151 source : DC1 128) chain B residue 24 type sequence G description BINDING SITE FOR RESIDUE XE B 1152 source : DC2 129) chain B residue 68 type sequence L description BINDING SITE FOR RESIDUE XE B 1152 source : DC2 130) chain D residue 71 type sequence F description BINDING SITE FOR RESIDUE XE D 1149 source : DC3 131) chain D residue 103 type sequence F description BINDING SITE FOR RESIDUE XE D 1149 source : DC3 132) chain D residue 106 type sequence L description BINDING SITE FOR RESIDUE XE D 1149 source : DC3 133) chain D residue 110 type sequence L description BINDING SITE FOR RESIDUE XE D 1149 source : DC3 134) chain D residue 24 type sequence G description BINDING SITE FOR RESIDUE XE D 1150 source : DC4 135) chain C residue 7 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 136) chain C residue 16 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 137) chain C residue 40 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 138) chain C residue 61 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 139) chain B residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 140) chain B residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 141) chain B residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 142) chain D residue 8 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 143) chain D residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 144) chain D residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 145) chain D residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 146) chain B residue 144 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI14 147) chain D residue 144 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI14 148) chain C residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 149) chain C residue 124 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 150) chain C residue 131 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 151) chain C residue 138 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 152) chain C residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 153) chain C residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 154) chain C residue 137 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 155) chain C residue 8 type SITE sequence T description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 156) chain C residue 91 type SITE sequence L description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 157) chain C residue 106 type SITE sequence L description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 158) chain C residue 108 type SITE sequence T description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 159) chain C residue 121 type SITE sequence V description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 160) chain C residue 133 type SITE sequence S description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 161) chain C residue 13 type SITE sequence A description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 162) chain C residue 24 type SITE sequence Y description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 163) chain C residue 29 type SITE sequence Y description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 164) chain C residue 45 type SITE sequence H description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 165) chain C residue 47 type SITE sequence D description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 166) chain C residue 52 type SITE sequence S description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 167) chain C residue 55 type SITE sequence V description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 168) chain C residue 59 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI3 169) chain C residue 11 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 170) chain B residue 74 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 171) chain B residue 84 type SITE sequence T description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 172) chain B residue 92 type SITE sequence H description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 173) chain B residue 104 type SITE sequence R description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 174) chain B residue 110 type SITE sequence L description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 175) chain B residue 119 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 176) chain B residue 122 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 177) chain B residue 128 type SITE sequence A description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 178) chain B residue 140 type SITE sequence A description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 179) chain B residue 144 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 180) chain C residue 56 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 181) chain D residue 7 type SITE sequence E description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 182) chain D residue 25 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 183) chain D residue 29 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 184) chain D residue 35 type SITE sequence Y description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 185) chain D residue 37 type SITE sequence W description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 186) chain D residue 45 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 187) chain D residue 52 type SITE sequence D description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 188) chain D residue 56 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 189) chain D residue 71 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 190) chain D residue 74 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 191) chain C residue 60 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 192) chain D residue 84 type SITE sequence T description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 193) chain D residue 92 type SITE sequence H description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 194) chain D residue 104 type SITE sequence R description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 195) chain D residue 110 type SITE sequence L description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 196) chain D residue 119 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 197) chain D residue 122 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 198) chain D residue 128 type SITE sequence A description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 199) chain D residue 140 type SITE sequence A description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 200) chain D residue 144 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 201) chain C residue 90 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 202) chain C residue 99 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 203) chain B residue 45 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 204) chain B residue 52 type SITE sequence D description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 205) chain B residue 56 type SITE sequence G description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 206) chain B residue 71 type SITE sequence F description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI4 207) chain C residue 3 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 208) chain C residue 35 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 209) chain C residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 210) chain D residue 59 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 211) chain D residue 82 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 212) chain D residue 95 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 213) chain C residue 7 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI6 214) chain C residue 16 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI6 215) chain C residue 40 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI6 216) chain C residue 8 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 217) chain B residue 44 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 218) chain D residue 9 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 219) chain D residue 44 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 220) chain C residue 11 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 221) chain B residue 50 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 222) chain B residue 87 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 223) chain D residue 12 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 224) chain D residue 50 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 225) chain D residue 87 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI8 226) chain C residue 24 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 227) chain B residue 82 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 228) chain D residue 59 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 229) chain D residue 82 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 230) chain C residue 58 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 231) chain B residue 2 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 232) chain B residue 82 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 233) chain B residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 234) chain D residue 1 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 235) chain D residue 2 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 236) chain D residue 82 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 237) chain D residue 143 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI1 238) chain C residue 87 type BINDING sequence H description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI2 239) chain D residue 63 type BINDING sequence Q description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238 source Swiss-Prot : SWS_FT_FI2

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