eF-site ID 1fdh-B PDB Code 1fdh Chain B click to enlarge Title STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN Classification OXYGEN TRANSPORT Compound HEMOGLOBIN F (DEOXY) (ALPHA CHAIN) Source Homo sapiens (Human) (HBG1_HUMAN) Sequence B:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR Description Functional site 1) chain B residue 42 type sequence Y description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 2) chain B residue 43 type sequence F description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 3) chain B residue 45 type sequence H description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 4) chain B residue 46 type sequence F description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 5) chain B residue 58 type sequence H description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 6) chain B residue 61 type sequence K description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 7) chain B residue 83 type sequence L description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 8) chain B residue 86 type sequence L description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 9) chain B residue 87 type sequence H description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 10) chain B residue 91 type sequence L description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 11) chain B residue 93 type sequence V description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 12) chain B residue 97 type sequence N description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 13) chain B residue 98 type sequence F description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 14) chain B residue 101 type sequence L description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 15) chain B residue 136 type sequence L description BINDING SITE FOR RESIDUE HEM B 142 source : AC3 16) chain B residue 72 type sequence H description BINDING SITE FOR RESIDUE HEM H 147 source : AC4 17) chain B residue 103 type MOD_RES sequence H description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 18) chain B residue 125 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 19) chain B residue 132 type MOD_RES sequence V description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 20) chain B residue 139 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI10 21) chain B residue 109 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 22) chain B residue 135 type MOD_RES sequence V description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 23) chain B residue 138 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:P01942 source Swiss-Prot : SWS_FT_FI11 24) chain B residue 9 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 14 type MOD_RES sequence W description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 25 type MOD_RES sequence G description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 30 type MOD_RES sequence E description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 46 type MOD_RES sequence F description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 48 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 53 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 56 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 60 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 92 type MOD_RES sequence R description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 107 type MOD_RES sequence V description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 109 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 122 type MOD_RES sequence H description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 134 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 17 type MOD_RES sequence V description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 39) chain B residue 41 type MOD_RES sequence T description S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 source Swiss-Prot : SWS_FT_FI6 40) chain B residue 8 type CARBOHYD sequence T description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 41) chain B residue 17 type CARBOHYD sequence V description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 42) chain B residue 41 type CARBOHYD sequence T description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI12 43) chain B residue 62 type CARBOHYD sequence V description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 source Swiss-Prot : SWS_FT_FI13 44) chain B residue 25 type MOD_RES sequence G description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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