eF-site ID 5ksi-ABCD PDB Code 5ksi Chain A, B, C, D click to enlarge Title Crystal structure of deoxygenated hemoglobin in complex with sphingosine phosphate and 2,3-Bisphosphoglycerate Classification OXYGEN TRANSPORT Compound Hemoglobin subunit alpha Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR B:  VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAHKYH C:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR D:  VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAHKYH Description Functional site 1) chain A residue 42 type sequence Y description binding site for residue HEM A 201 source : AC1 2) chain A residue 43 type sequence F description binding site for residue HEM A 201 source : AC1 3) chain A residue 45 type sequence H description binding site for residue HEM A 201 source : AC1 4) chain A residue 46 type sequence F description binding site for residue HEM A 201 source : AC1 5) chain A residue 58 type sequence H description binding site for residue HEM A 201 source : AC1 6) chain A residue 61 type sequence K description binding site for residue HEM A 201 source : AC1 7) chain A residue 83 type sequence L description binding site for residue HEM A 201 source : AC1 8) chain A residue 86 type sequence L description binding site for residue HEM A 201 source : AC1 9) chain A residue 87 type sequence H description binding site for residue HEM A 201 source : AC1 10) chain A residue 91 type sequence L description binding site for residue HEM A 201 source : AC1 11) chain A residue 93 type sequence V description binding site for residue HEM A 201 source : AC1 12) chain A residue 97 type sequence N description binding site for residue HEM A 201 source : AC1 13) chain A residue 98 type sequence F description binding site for residue HEM A 201 source : AC1 14) chain A residue 101 type sequence L description binding site for residue HEM A 201 source : AC1 15) chain A residue 136 type sequence L description binding site for residue HEM A 201 source : AC1 16) chain D residue 17 type sequence K description binding site for residue HEM A 201 source : AC1 17) chain A residue 36 type sequence F description binding site for residue S1P A 202 source : AC2 18) chain A residue 99 type sequence K description binding site for residue S1P A 202 source : AC2 19) chain A residue 100 type sequence L description binding site for residue S1P A 202 source : AC2 20) chain A residue 103 type sequence H description binding site for residue S1P A 202 source : AC2 21) chain B residue 108 type sequence N description binding site for residue S1P A 202 source : AC2 22) chain A residue 41 type sequence T description binding site for residue S1P A 203 source : AC3 23) chain A residue 42 type sequence Y description binding site for residue S1P A 203 source : AC3 24) chain A residue 44 type sequence P description binding site for residue S1P A 203 source : AC3 25) chain A residue 45 type sequence H description binding site for residue S1P A 203 source : AC3 26) chain A residue 90 type sequence K description binding site for residue S1P A 203 source : AC3 27) chain A residue 91 type sequence L description binding site for residue S1P A 203 source : AC3 28) chain A residue 92 type sequence R description binding site for residue S1P A 203 source : AC3 29) chain D residue 40 type sequence R description binding site for residue S1P A 203 source : AC3 30) chain D residue 41 type sequence F description binding site for residue S1P A 203 source : AC3 31) chain D residue 96 type sequence L description binding site for residue S1P A 203 source : AC3 32) chain D residue 97 type sequence H description binding site for residue S1P A 203 source : AC3 33) chain A residue 56 type sequence K description binding site for residue HEM B 201 source : AC4 34) chain B residue 63 type sequence H description binding site for residue HEM B 201 source : AC4 35) chain B residue 66 type sequence K description binding site for residue HEM B 201 source : AC4 36) chain B residue 67 type sequence V description binding site for residue HEM B 201 source : AC4 37) chain B residue 91 type sequence L description binding site for residue HEM B 201 source : AC4 38) chain B residue 92 type sequence H description binding site for residue HEM B 201 source : AC4 39) chain B residue 96 type sequence L description binding site for residue HEM B 201 source : AC4 40) chain B residue 102 type sequence N description binding site for residue HEM B 201 source : AC4 41) chain B residue 103 type sequence F description binding site for residue HEM B 201 source : AC4 42) chain B residue 141 type sequence L description binding site for residue HEM B 201 source : AC4 43) chain B residue 82 type sequence K description binding site for residue DG2 B 202 source : AC5 44) chain C residue 32 type sequence M description binding site for residue HEM C 201 source : AC6 45) chain C residue 42 type sequence Y description binding site for residue HEM C 201 source : AC6 46) chain C residue 43 type sequence F description binding site for residue HEM C 201 source : AC6 47) chain C residue 45 type sequence H description binding site for residue HEM C 201 source : AC6 48) chain C residue 46 type sequence F description binding site for residue HEM C 201 source : AC6 49) chain C residue 58 type sequence H description binding site for residue HEM C 201 source : AC6 50) chain C residue 61 type sequence K description binding site for residue HEM C 201 source : AC6 51) chain C residue 83 type sequence L description binding site for residue HEM C 201 source : AC6 52) chain C residue 86 type sequence L description binding site for residue HEM C 201 source : AC6 53) chain C residue 87 type sequence H description binding site for residue HEM C 201 source : AC6 54) chain C residue 91 type sequence L description binding site for residue HEM C 201 source : AC6 55) chain C residue 93 type sequence V description binding site for residue HEM C 201 source : AC6 56) chain C residue 97 type sequence N description binding site for residue HEM C 201 source : AC6 57) chain C residue 98 type sequence F description binding site for residue HEM C 201 source : AC6 58) chain C residue 101 type sequence L description binding site for residue HEM C 201 source : AC6 59) chain C residue 136 type sequence L description binding site for residue HEM C 201 source : AC6 60) chain C residue 36 type sequence F description binding site for residue S1P C 202 source : AC7 61) chain C residue 99 type sequence K description binding site for residue S1P C 202 source : AC7 62) chain C residue 100 type sequence L description binding site for residue S1P C 202 source : AC7 63) chain C residue 103 type sequence H description binding site for residue S1P C 202 source : AC7 64) chain D residue 108 type sequence N description binding site for residue S1P C 202 source : AC7 65) chain D residue 131 type sequence Q description binding site for residue S1P C 202 source : AC7 66) chain B residue 40 type sequence R description binding site for residue S1P C 203 source : AC8 67) chain B residue 97 type sequence H description binding site for residue S1P C 203 source : AC8 68) chain C residue 41 type sequence T description binding site for residue S1P C 203 source : AC8 69) chain C residue 42 type sequence Y description binding site for residue S1P C 203 source : AC8 70) chain C residue 44 type sequence P description binding site for residue S1P C 203 source : AC8 71) chain C residue 90 type sequence K description binding site for residue S1P C 203 source : AC8 72) chain C residue 91 type sequence L description binding site for residue S1P C 203 source : AC8 73) chain C residue 92 type sequence R description binding site for residue S1P C 203 source : AC8 74) chain C residue 72 type sequence H description binding site for residue HEM D 201 source : AC9 75) chain D residue 41 type sequence F description binding site for residue HEM D 201 source : AC9 76) chain D residue 42 type sequence F description binding site for residue HEM D 201 source : AC9 77) chain D residue 63 type sequence H description binding site for residue HEM D 201 source : AC9 78) chain D residue 66 type sequence K description binding site for residue HEM D 201 source : AC9 79) chain D residue 67 type sequence V description binding site for residue HEM D 201 source : AC9 80) chain D residue 91 type sequence L description binding site for residue HEM D 201 source : AC9 81) chain D residue 92 type sequence H description binding site for residue HEM D 201 source : AC9 82) chain D residue 96 type sequence L description binding site for residue HEM D 201 source : AC9 83) chain D residue 102 type sequence N description binding site for residue HEM D 201 source : AC9 84) chain D residue 103 type sequence F description binding site for residue HEM D 201 source : AC9 85) chain D residue 141 type sequence L description binding site for residue HEM D 201 source : AC9 86) chain A residue 41 type sequence T description binding site for residue S1P D 202 source : AD1 87) chain A residue 42 type sequence Y description binding site for residue S1P D 202 source : AD1 88) chain A residue 45 type sequence H description binding site for residue S1P D 202 source : AD1 89) chain A residue 90 type sequence K description binding site for residue S1P D 202 source : AD1 90) chain A residue 91 type sequence L description binding site for residue S1P D 202 source : AD1 91) chain C residue 72 type sequence H description binding site for residue S1P D 202 source : AD1 92) chain D residue 40 type sequence R description binding site for residue S1P D 202 source : AD1 93) chain D residue 41 type sequence F description binding site for residue S1P D 202 source : AD1 94) chain D residue 96 type sequence L description binding site for residue S1P D 202 source : AD1 95) chain D residue 97 type sequence H description binding site for residue S1P D 202 source : AD1 96) chain D residue 120 type sequence K description binding site for residue S1P D 202 source : AD1 97) chain B residue 82 type sequence K description binding site for residue DG2 D 203 source : AD2 98) chain D residue 1 type sequence V description binding site for residue DG2 D 203 source : AD2 99) chain D residue 82 type sequence K description binding site for residue DG2 D 203 source : AD2 100) chain A residue 40 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 101) chain C residue 7 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 102) chain C residue 16 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 103) chain C residue 40 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 104) chain B residue 1 type CARBOHYD sequence V description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 105) chain D residue 1 type CARBOHYD sequence V description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 106) chain B residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 107) chain B residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 108) chain D residue 8 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 109) chain D residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 110) chain D residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 111) chain D residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 112) chain B residue 8 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 113) chain B residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 114) 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 115) 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 116) chain B residue 82 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 117) chain B residue 143 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 118) chain D residue 1 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 119) chain D residue 2 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 120) chain D residue 82 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 121) chain D residue 143 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 122) chain B residue 1 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 123) chain B residue 2 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 124) chain B residue 63 type BINDING sequence H description distal binding residue source Swiss-Prot : SWS_FT_FI2 125) chain D residue 63 type BINDING sequence H description distal binding residue source Swiss-Prot : SWS_FT_FI2 126) chain B residue 92 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 127) chain D residue 92 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 128) chain A residue 24 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 129) chain A residue 29 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 130) chain A residue 45 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 131) chain A residue 47 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 132) chain A residue 52 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 133) chain A residue 55 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 134) chain A residue 59 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 135) chain A residue 91 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 136) chain A residue 106 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 137) chain A residue 108 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 138) chain A residue 121 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 139) chain A residue 133 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 140) chain C residue 8 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 141) chain C residue 13 type BINDING sequence A description proximal binding residue source Swiss-Prot : SWS_FT_FI3 142) chain C residue 24 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 143) chain C residue 29 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 144) chain C residue 45 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 145) chain C residue 47 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 146) chain C residue 52 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 147) chain C residue 55 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 148) chain C residue 59 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 149) chain C residue 91 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 150) chain C residue 106 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 151) chain C residue 108 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 152) chain C residue 121 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 153) chain C residue 133 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 154) chain B residue 84 type SITE sequence T description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 155) chain B residue 92 type SITE sequence H description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 156) chain B residue 104 type SITE sequence R description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 157) chain B residue 110 type SITE sequence L description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 158) chain B residue 119 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 159) chain B residue 122 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 160) chain B residue 128 type SITE sequence A description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 161) chain B residue 140 type SITE sequence A description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 162) chain B residue 144 type SITE sequence K description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 163) chain D residue 7 type SITE sequence E description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 164) chain D residue 25 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 165) chain D residue 29 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 166) chain D residue 35 type SITE sequence Y description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 167) chain D residue 37 type SITE sequence W description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 168) chain D residue 45 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 169) chain D residue 52 type SITE sequence D description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 170) chain D residue 56 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 171) chain D residue 71 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 172) chain D residue 74 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 173) chain D residue 84 type SITE sequence T description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 174) chain D residue 92 type SITE sequence H description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 175) chain D residue 104 type SITE sequence R description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 176) chain D residue 110 type SITE sequence L description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 177) chain D residue 119 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 178) chain D residue 122 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 179) chain D residue 128 type SITE sequence A description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 180) chain D residue 140 type SITE sequence A description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 181) chain D residue 144 type SITE sequence K description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 182) chain B residue 52 type SITE sequence D description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 183) chain B residue 56 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 184) chain B residue 71 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 185) chain B residue 74 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 186) chain B residue 7 type SITE sequence E description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 187) chain B residue 25 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 188) chain B residue 29 type SITE sequence G description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 189) chain B residue 35 type SITE sequence Y description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 190) chain B residue 37 type SITE sequence W description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 191) chain B residue 45 type SITE sequence F description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 source Swiss-Prot : SWS_FT_FI4 192) chain B residue 59 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 193) chain B residue 82 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 194) chain B residue 95 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 195) chain D residue 59 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 196) chain D residue 82 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 197) chain D residue 95 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 198) chain B residue 1 type MOD_RES sequence V description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 199) chain D residue 1 type MOD_RES sequence V description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 200) chain A residue 40 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 201) chain C residue 7 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 202) chain C residue 16 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 203) chain C residue 40 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 204) chain D residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 205) chain D residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 206) chain B residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 207) chain B residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 208) chain D residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 209) chain D residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 210) chain B residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 211) chain D residue 12 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 212) chain B residue 12 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 213) chain B residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 214) chain D residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 215) chain D residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 216) chain B residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 217) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 218) chain C residue 131 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 219) chain C residue 138 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 220) chain B residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 221) chain D residue 93 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 222) chain A residue 131 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 223) chain A residue 138 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 224) chain C residue 102 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 225) chain C residue 124 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 226) chain A residue 137 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 227) chain C residue 108 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 228) chain C residue 134 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 229) chain C residue 137 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 230) chain B residue 144 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 231) chain D residue 144 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11

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