eF-site ID 5o10-AB PDB Code 5o10 Chain A, B click to enlarge Title Y48H mutant of human cytochrome c Classification ELECTRON TRANSFER, APOPTOSIS Compound Cytochrome c Source Homo sapiens (Human) (CYC_HUMAN) Sequence A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSHTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE B:  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 29 type sequence G description binding site for residue HEC A 201 source : AC1 7) chain A residue 30 type sequence P description binding site for residue HEC A 201 source : AC1 8) chain A residue 38 type sequence R 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 67 type sequence Y description binding site for residue HEC A 201 source : AC1 16) chain A residue 78 type sequence T description binding site for residue HEC A 201 source : AC1 17) chain A residue 79 type sequence K description binding site for residue HEC A 201 source : AC1 18) chain A residue 80 type sequence M description binding site for residue HEC A 201 source : AC1 19) chain A residue 81 type sequence I description binding site for residue HEC A 201 source : AC1 20) chain A residue 82 type sequence F description binding site for residue HEC A 201 source : AC1 21) chain A residue 55 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 22) chain B residue 13 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 23) chain B residue 14 type sequence C description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 24) chain B residue 15 type sequence S description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 25) chain B residue 16 type sequence Q description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 26) chain B residue 18 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 27) chain B residue 27 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 28) chain B residue 28 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 29) chain B residue 29 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 30) chain B residue 30 type sequence P description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 31) chain B residue 38 type sequence R description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 32) chain B residue 41 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 33) chain B residue 46 type sequence Y description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 34) chain B residue 48 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 35) chain B residue 49 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 36) chain B residue 52 type sequence N description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 37) chain B residue 59 type sequence W description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 38) chain B residue 78 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 39) chain B residue 79 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 40) chain B residue 80 type sequence M description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 41) chain B residue 81 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 42) chain B residue 82 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 43) chain B residue 85 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 44) chain A residue 55 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 45) chain B residue 10 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 46) chain B residue 13 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 47) chain B residue 15 type sequence S description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 48) chain B residue 16 type sequence Q description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 49) chain B residue 17 type sequence C description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 50) chain B residue 18 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 51) chain B residue 28 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 52) chain B residue 29 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 53) chain B residue 30 type sequence P description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 54) chain B residue 38 type sequence R description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 55) chain B residue 41 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 56) chain B residue 46 type sequence Y description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 57) chain B residue 48 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 58) chain B residue 49 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 59) chain B residue 52 type sequence N description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 60) chain B residue 59 type sequence W description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 61) chain B residue 78 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 62) chain B residue 79 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 63) chain B residue 80 type sequence M description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 64) chain B residue 81 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 65) chain B residue 82 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 66) chain B residue 85 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 67) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 68) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 69) chain B residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 71) 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 72) 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 73) 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 74) chain B 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 75) chain A residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 76) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 77) chain A residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 78) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 79) chain B residue 48 type MOD_RES sequence H description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 80) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 81) chain A residue 48 type MOD_RES sequence H description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 82) chain A residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 83) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 84) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 85) chain A residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 86) chain B residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7

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