eF-site ID 5exq-A PDB Code 5exq Chain A click to enlarge Title Human cytochrome c Y48H Classification APOPTOSIS Compound Cytochrome c Source (CYC_HUMAN) Sequence A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSHTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain A residue 13 type sequence K description binding site for residue HEC A 201 source : AC1 2) chain A residue 14 type sequence C description binding site for residue HEC A 201 source : AC1 3) chain A residue 17 type sequence C description binding site for residue HEC A 201 source : AC1 4) chain A residue 18 type sequence H description binding site for residue HEC A 201 source : AC1 5) chain A residue 28 type sequence T description binding site for residue HEC A 201 source : AC1 6) chain A residue 30 type sequence P description binding site for residue HEC A 201 source : AC1 7) chain A residue 38 type sequence R description binding site for residue HEC A 201 source : AC1 8) chain A residue 40 type sequence T description binding site for residue HEC A 201 source : AC1 9) chain A residue 41 type sequence G description binding site for residue HEC A 201 source : AC1 10) chain A residue 46 type sequence Y description binding site for residue HEC A 201 source : AC1 11) chain A residue 48 type sequence H description binding site for residue HEC A 201 source : AC1 12) chain A residue 49 type sequence T description binding site for residue HEC A 201 source : AC1 13) chain A residue 52 type sequence N description binding site for residue HEC A 201 source : AC1 14) chain A residue 59 type sequence W description binding site for residue HEC A 201 source : AC1 15) chain A residue 78 type sequence T description binding site for residue HEC A 201 source : AC1 16) chain A residue 79 type sequence K description binding site for residue HEC A 201 source : AC1 17) chain A residue 80 type sequence M description binding site for residue HEC A 201 source : AC1 18) chain A residue 81 type sequence I description binding site for residue HEC A 201 source : AC1 19) chain A residue 82 type sequence F description binding site for residue HEC A 201 source : AC1 20) chain A residue 36 type sequence F description binding site for residue SO4 B 202 source : AC2 21) chain A residue 60 type sequence G description binding site for residue SO4 B 202 source : AC2 22) chain A residue 61 type sequence E description binding site for residue SO4 B 202 source : AC2 23) chain A residue 99 type sequence K description binding site for residue SO4 B 202 source : AC2 24) chain A residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 26) chain A 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 27) chain A residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 28) chain A residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 48 type MOD_RES sequence H description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8

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