eF-site ID 6ecj-G PDB Code 6ecj Chain G click to enlarge Title Human cytochrome c G41T Classification APOPTOSIS Compound Cytochrome c Source (CYC_HUMAN) Sequence G:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT TQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain G residue 13 type sequence K description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 2) chain G residue 14 type sequence C description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 3) chain G residue 15 type sequence S description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 4) chain G residue 16 type sequence Q description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 5) chain G residue 18 type sequence H description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 6) chain G residue 27 type sequence K description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 7) chain G residue 28 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 8) chain G residue 29 type sequence G description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 9) chain G residue 30 type sequence P description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 10) chain G residue 40 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 11) chain G residue 41 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 12) chain G residue 46 type sequence Y description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 13) chain G residue 48 type sequence Y description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 14) chain G residue 49 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 15) chain G residue 52 type sequence N description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 16) chain G residue 59 type sequence W description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 17) chain G residue 68 type sequence L description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 18) chain G residue 78 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 19) chain G residue 79 type sequence K description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 20) chain G residue 80 type sequence M description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 21) chain G residue 94 type sequence L description binding site for Di-peptide HEM G 201 and CYS G 17 source : AD3 22) chain G residue 10 type sequence F description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 23) chain G residue 13 type sequence K description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 24) chain G residue 15 type sequence S description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 25) chain G residue 16 type sequence Q description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 26) chain G residue 17 type sequence C description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 27) chain G residue 18 type sequence H description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 28) chain G residue 28 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 29) chain G residue 29 type sequence G description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 30) chain G residue 30 type sequence P description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 31) chain G residue 40 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 32) chain G residue 41 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 33) chain G residue 46 type sequence Y description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 34) chain G residue 48 type sequence Y description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 35) chain G residue 49 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 36) chain G residue 52 type sequence N description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 37) chain G residue 59 type sequence W description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 38) chain G residue 68 type sequence L description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 39) chain G residue 78 type sequence T description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 40) chain G residue 79 type sequence K description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 41) chain G residue 80 type sequence M description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 42) chain G residue 94 type sequence L description binding site for Di-peptide HEM G 201 and CYS G 14 source : AD4 43) chain G residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 44) chain G residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 45) chain G residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 46) chain G residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 47) chain G residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 48) chain G residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 49) chain G residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 50) chain G residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 51) chain G 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 52) chain G residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3

Display surface Download Links