eF-site ID 6nbd_5-ABCD PDB Code 6nbd Model 5 Chain A, B, C, D click to enlarge Title Human methemoglobin state 2 determined using single-particle cryo-EM at 200 keV Classification OXYGEN TRANSPORT Compound Hemoglobin subunit alpha Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKY B:  VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAH C:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKY D:  VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAH 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 87 type sequence H description binding site for residue HEM A 201 source : AC1 9) chain A residue 91 type sequence L description binding site for residue HEM A 201 source : AC1 10) chain A residue 97 type sequence N description binding site for residue HEM A 201 source : AC1 11) chain A residue 98 type sequence F description binding site for residue HEM A 201 source : AC1 12) chain A residue 101 type sequence L description binding site for residue HEM A 201 source : AC1 13) chain A residue 136 type sequence L description binding site for residue HEM A 201 source : AC1 14) chain B residue 38 type sequence T description binding site for residue HEM B 201 source : AC2 15) chain B residue 41 type sequence F description binding site for residue HEM B 201 source : AC2 16) chain B residue 42 type sequence F description binding site for residue HEM B 201 source : AC2 17) chain B residue 63 type sequence H description binding site for residue HEM B 201 source : AC2 18) chain B residue 66 type sequence K description binding site for residue HEM B 201 source : AC2 19) chain B residue 70 type sequence A description binding site for residue HEM B 201 source : AC2 20) chain B residue 92 type sequence H description binding site for residue HEM B 201 source : AC2 21) chain B residue 96 type sequence L description binding site for residue HEM B 201 source : AC2 22) chain B residue 102 type sequence N description binding site for residue HEM B 201 source : AC2 23) chain B residue 103 type sequence F description binding site for residue HEM B 201 source : AC2 24) chain B residue 106 type sequence L description binding site for residue HEM B 201 source : AC2 25) chain B residue 141 type sequence L description binding site for residue HEM B 201 source : AC2 26) chain C residue 42 type sequence Y description binding site for residue HEM C 201 source : AC3 27) chain C residue 43 type sequence F description binding site for residue HEM C 201 source : AC3 28) chain C residue 45 type sequence H description binding site for residue HEM C 201 source : AC3 29) chain C residue 46 type sequence F description binding site for residue HEM C 201 source : AC3 30) chain C residue 58 type sequence H description binding site for residue HEM C 201 source : AC3 31) chain C residue 61 type sequence K description binding site for residue HEM C 201 source : AC3 32) chain C residue 83 type sequence L description binding site for residue HEM C 201 source : AC3 33) chain C residue 86 type sequence L description binding site for residue HEM C 201 source : AC3 34) chain C residue 87 type sequence H description binding site for residue HEM C 201 source : AC3 35) chain C residue 91 type sequence L description binding site for residue HEM C 201 source : AC3 36) chain C residue 97 type sequence N description binding site for residue HEM C 201 source : AC3 37) chain C residue 98 type sequence F description binding site for residue HEM C 201 source : AC3 38) chain C residue 101 type sequence L description binding site for residue HEM C 201 source : AC3 39) chain C residue 132 type sequence V description binding site for residue HEM C 201 source : AC3 40) chain C residue 136 type sequence L description binding site for residue HEM C 201 source : AC3 41) chain D residue 38 type sequence T description binding site for residue HEM D 201 source : AC4 42) chain D residue 41 type sequence F description binding site for residue HEM D 201 source : AC4 43) chain D residue 42 type sequence F description binding site for residue HEM D 201 source : AC4 44) chain D residue 63 type sequence H description binding site for residue HEM D 201 source : AC4 45) chain D residue 66 type sequence K description binding site for residue HEM D 201 source : AC4 46) chain D residue 70 type sequence A description binding site for residue HEM D 201 source : AC4 47) chain D residue 71 type sequence F description binding site for residue HEM D 201 source : AC4 48) chain D residue 92 type sequence H description binding site for residue HEM D 201 source : AC4 49) chain D residue 96 type sequence L description binding site for residue HEM D 201 source : AC4 50) chain D residue 102 type sequence N description binding site for residue HEM D 201 source : AC4 51) chain D residue 103 type sequence F description binding site for residue HEM D 201 source : AC4 52) chain D residue 106 type sequence L description binding site for residue HEM D 201 source : AC4 53) chain D residue 137 type sequence V description binding site for residue HEM D 201 source : AC4 54) chain D residue 141 type sequence L description binding site for residue HEM D 201 source : AC4 55) chain A residue 61 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 56) chain C residue 61 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 57) chain B residue 1 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 58) chain B residue 2 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 59) chain B residue 82 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 60) chain B residue 143 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 61) chain D residue 1 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 62) chain D residue 2 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 63) chain D residue 82 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI1 64) chain D residue 143 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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_FI11 74) 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_FI11 75) chain A residue 137 type CARBOHYD sequence T description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI11 76) chain C residue 108 type CARBOHYD sequence T description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI11 77) chain C residue 134 type CARBOHYD sequence T description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI11 78) chain C residue 137 type CARBOHYD sequence T description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI11 79) chain B residue 63 type BINDING sequence H description distal binding residue source Swiss-Prot : SWS_FT_FI2 80) chain D residue 63 type BINDING sequence H description distal binding residue source Swiss-Prot : SWS_FT_FI2 81) chain B residue 92 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 82) chain A residue 91 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 83) chain A residue 106 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 84) chain A residue 108 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 85) chain A residue 121 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 86) chain A residue 133 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 87) chain C residue 8 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 88) chain C residue 13 type BINDING sequence A description proximal binding residue source Swiss-Prot : SWS_FT_FI3 89) chain C residue 24 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 90) chain C residue 29 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 91) chain C residue 45 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 92) chain D residue 92 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 93) chain C residue 47 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 94) chain C residue 52 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 95) chain C residue 55 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 96) chain C residue 59 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 97) chain C residue 91 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 98) chain C residue 106 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 99) chain C residue 108 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 100) chain C residue 121 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 101) chain C residue 133 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 102) chain A residue 24 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 103) chain A residue 29 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 104) chain A residue 45 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 105) chain A residue 47 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 106) chain A residue 52 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 107) chain A residue 55 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 108) chain A residue 59 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 109) 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 110) 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 111) 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 112) 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 113) 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 114) 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 115) 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 116) 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 117) 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 118) 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 119) 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 120) 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 121) 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 122) 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 123) 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 124) 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 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) 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 138) 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 139) 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 140) 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 141) 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 142) 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 143) 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 144) 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 145) chain B residue 59 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 146) chain B residue 82 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 147) chain B residue 95 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 148) chain D residue 59 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 149) chain D residue 82 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 150) chain D residue 95 type SITE sequence K description Not glycated => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI5 151) chain B residue 1 type MOD_RES sequence V description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 152) chain D residue 1 type MOD_RES sequence V description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 153) chain A residue 40 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 154) chain C residue 7 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 155) chain C residue 16 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 156) chain C residue 40 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 157) chain B residue 8 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 158) chain B residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 159) chain B residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 160) chain B residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 161) chain D residue 8 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 162) chain D residue 17 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 163) chain D residue 66 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 164) chain D residue 120 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 165) chain B residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 166) chain B residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 167) chain D residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 168) chain D residue 44 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 169) chain B residue 12 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 170) chain B residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 171) chain B residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 172) chain D residue 12 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 173) chain D residue 50 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 174) chain D residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 175) chain B residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 176) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 177) chain D residue 59 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9 178) chain D residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links