eF-site ID 5ksi-A PDB Code 5ksi Chain A 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 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 A residue 36 type sequence F description binding site for residue S1P A 202 source : AC2 17) chain A residue 99 type sequence K description binding site for residue S1P A 202 source : AC2 18) chain A residue 100 type sequence L description binding site for residue S1P A 202 source : AC2 19) chain A residue 103 type sequence H description binding site for residue S1P A 202 source : AC2 20) chain A residue 41 type sequence T description binding site for residue S1P A 203 source : AC3 21) chain A residue 42 type sequence Y description binding site for residue S1P A 203 source : AC3 22) chain A residue 44 type sequence P description binding site for residue S1P A 203 source : AC3 23) chain A residue 45 type sequence H description binding site for residue S1P A 203 source : AC3 24) chain A residue 90 type sequence K description binding site for residue S1P A 203 source : AC3 25) chain A residue 91 type sequence L description binding site for residue S1P A 203 source : AC3 26) chain A residue 92 type sequence R description binding site for residue S1P A 203 source : AC3 27) chain A residue 56 type sequence K description binding site for residue HEM B 201 source : AC4 28) chain A residue 41 type sequence T description binding site for residue S1P D 202 source : AD1 29) chain A residue 42 type sequence Y description binding site for residue S1P D 202 source : AD1 30) chain A residue 45 type sequence H description binding site for residue S1P D 202 source : AD1 31) chain A residue 90 type sequence K description binding site for residue S1P D 202 source : AD1 32) chain A residue 91 type sequence L description binding site for residue S1P D 202 source : AD1 33) chain A residue 137 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 34) 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 35) chain A residue 91 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 36) chain A residue 106 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 37) chain A residue 108 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 38) chain A residue 121 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 39) chain A residue 133 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 40) chain A residue 24 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 41) chain A residue 29 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 42) chain A residue 45 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 43) chain A residue 47 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 44) chain A residue 52 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 45) chain A residue 55 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 46) chain A residue 59 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 47) chain A residue 40 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 48) 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 49) 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

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