eF-site ID 6ecj-E PDB Code 6ecj Chain E click to enlarge Title Human cytochrome c G41T Classification APOPTOSIS Compound Cytochrome c Source (CYC_HUMAN) Sequence E:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT TQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain E residue 13 type sequence K description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 2) chain E residue 14 type sequence C description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 3) chain E residue 15 type sequence S description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 4) chain E residue 16 type sequence Q description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 5) chain E residue 18 type sequence H description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 6) chain E residue 27 type sequence K description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 7) chain E residue 28 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 8) chain E residue 29 type sequence G description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 9) chain E residue 30 type sequence P description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 10) chain E residue 35 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 11) chain E residue 40 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 12) chain E residue 41 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 13) chain E residue 46 type sequence Y description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 14) chain E residue 48 type sequence Y description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 15) chain E residue 49 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 16) chain E residue 52 type sequence N description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 17) chain E residue 59 type sequence W description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 18) chain E residue 68 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 19) chain E residue 78 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 20) chain E residue 79 type sequence K description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 21) chain E residue 80 type sequence M description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 22) chain E residue 94 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 17 source : AC8 23) chain E residue 10 type sequence F description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 24) chain E residue 13 type sequence K description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 25) chain E residue 15 type sequence S description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 26) chain E residue 16 type sequence Q description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 27) chain E residue 17 type sequence C description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 28) chain E residue 18 type sequence H description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 29) chain E residue 28 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 30) chain E residue 29 type sequence G description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 31) chain E residue 30 type sequence P description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 32) chain E residue 35 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 33) chain E residue 40 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 34) chain E residue 41 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 35) chain E residue 46 type sequence Y description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 36) chain E residue 48 type sequence Y description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 37) chain E residue 49 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 38) chain E residue 52 type sequence N description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 39) chain E residue 59 type sequence W description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 40) chain E residue 68 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 41) chain E residue 78 type sequence T description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 42) chain E residue 79 type sequence K description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 43) chain E residue 80 type sequence M description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 44) chain E residue 94 type sequence L description binding site for Di-peptide HEM E 201 and CYS E 14 source : AC9 45) chain E residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 46) chain E residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 47) chain E residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 48) chain E residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 49) chain E residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 50) chain E residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 51) chain E residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 52) chain E residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 53) chain E residue 18 type BINDING sequence H description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI2 54) chain E residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3

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