eF-site ID 5o10-B PDB Code 5o10 Chain 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 B:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSHTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain B residue 13 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 2) chain B residue 14 type sequence C description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 3) chain B residue 15 type sequence S description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 4) chain B residue 16 type sequence Q description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 5) chain B residue 18 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 6) chain B residue 27 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 7) chain B residue 28 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 8) chain B residue 29 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 9) chain B residue 30 type sequence P description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 10) chain B residue 38 type sequence R description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 11) chain B residue 41 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 12) chain B residue 46 type sequence Y description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 13) chain B residue 48 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 14) chain B residue 49 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 15) chain B residue 52 type sequence N description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 16) chain B residue 59 type sequence W description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 17) chain B residue 78 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 18) chain B residue 79 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 19) chain B residue 80 type sequence M description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 20) chain B residue 81 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 21) chain B residue 82 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 22) chain B residue 85 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 17 source : AC2 23) chain B residue 10 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 24) chain B residue 13 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 25) chain B residue 15 type sequence S description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 26) chain B residue 16 type sequence Q description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 27) chain B residue 17 type sequence C description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 28) chain B residue 18 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 29) chain B residue 28 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 30) chain B residue 29 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 31) chain B residue 30 type sequence P description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 32) chain B residue 38 type sequence R description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 33) chain B residue 41 type sequence G description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 34) chain B residue 46 type sequence Y description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 35) chain B residue 48 type sequence H description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 36) chain B residue 49 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 37) chain B residue 52 type sequence N description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 38) chain B residue 59 type sequence W description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 39) chain B residue 78 type sequence T description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 40) chain B residue 79 type sequence K description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 41) chain B residue 80 type sequence M description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 42) chain B residue 81 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 43) chain B residue 82 type sequence F description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 44) chain B residue 85 type sequence I description binding site for Di-peptide HEC B 201 and CYS B 14 source : AC3 45) chain B residue 48 type MOD_RES sequence H description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 46) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 47) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 48) chain B residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 49) 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 50) 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 51) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 52) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 53) 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 54) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3

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