eF-site ID 3kmf-E PDB Code 3kmf Chain E click to enlarge Title Room Temperature Time-of-Flight Neutron Diffraction Study of Deoxy Human Normal Adult Hemoglobin Classification OXYGEN STORAGE, OXYGEN TRANSPORT Compound Hemoglobin subunit alpha Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence E:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR Description Functional site 1) chain E residue 442 type sequence Y description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 2) chain E residue 443 type sequence F description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 3) chain E residue 445 type sequence H description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 4) chain E residue 458 type sequence H description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 5) chain E residue 461 type sequence K description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 6) chain E residue 486 type sequence L description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 7) chain E residue 487 type sequence H description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 8) chain E residue 491 type sequence L description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 9) chain E residue 497 type sequence N description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 10) chain E residue 498 type sequence F description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 11) chain E residue 536 type sequence L description BINDING SITE FOR RESIDUE HEM E 542 source : AC3 12) chain E residue 408 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 13) chain E residue 413 type BINDING sequence A description proximal binding residue source Swiss-Prot : SWS_FT_FI3 14) chain E residue 424 type BINDING sequence Y description proximal binding residue source Swiss-Prot : SWS_FT_FI3 15) chain E residue 429 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 16) chain E residue 445 type BINDING sequence H description proximal binding residue source Swiss-Prot : SWS_FT_FI3 17) chain E residue 447 type BINDING sequence D description proximal binding residue source Swiss-Prot : SWS_FT_FI3 18) chain E residue 452 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 19) chain E residue 455 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 20) chain E residue 459 type BINDING sequence G description proximal binding residue source Swiss-Prot : SWS_FT_FI3 21) chain E residue 491 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 22) chain E residue 506 type BINDING sequence L description proximal binding residue source Swiss-Prot : SWS_FT_FI3 23) chain E residue 508 type BINDING sequence T description proximal binding residue source Swiss-Prot : SWS_FT_FI3 24) chain E residue 521 type BINDING sequence V description proximal binding residue source Swiss-Prot : SWS_FT_FI3 25) chain E residue 533 type BINDING sequence S description proximal binding residue source Swiss-Prot : SWS_FT_FI3 26) chain E residue 407 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 27) chain E residue 416 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 28) chain E residue 440 type MOD_RES sequence K description N-pyruvate 2-iminyl-valine; in Hb A1b source Swiss-Prot : SWS_FT_FI6 29) chain E residue 502 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 30) chain E residue 524 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 31) chain E residue 531 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 32) chain E residue 538 type MOD_RES sequence S description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 source Swiss-Prot : SWS_FT_FI10 33) chain E residue 508 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 34) chain E residue 534 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 35) chain E residue 537 type MOD_RES sequence T description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 source Swiss-Prot : SWS_FT_FI11 36) chain E residue 407 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 37) chain E residue 416 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12 38) chain E residue 440 type CARBOHYD sequence K description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 source Swiss-Prot : SWS_FT_FI12

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