eF-site ID 5df5-C PDB Code 5df5 Chain C click to enlarge Title The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution. Classification ELECTRON TRANSPORT Compound Cytochrome c, somatic Source Rattus norvegicus (Rat) (CYC_RAT) Sequence C:  GDVEKGKKIFVQKCAQCHTVEKGGKHKEGPNLHGLFGRKT GQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKM IFAGIKKKGERADLIAYLKKATNE Description Functional site 1) chain C residue 87 type sequence K description binding site for residue FC6 C 202 source : AC4 2) chain C residue 88 type sequence K description binding site for residue FC6 C 202 source : AC4 3) chain C residue 89 type sequence G description binding site for residue FC6 C 202 source : AC4 4) chain C residue 13 type sequence K description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 5) chain C residue 14 type sequence C description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 6) chain C residue 15 type sequence A description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 7) chain C residue 16 type sequence Q description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 8) chain C residue 18 type sequence H description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 9) chain C residue 27 type sequence K description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 10) chain C residue 28 type sequence E description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 11) chain C residue 29 type sequence G description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 12) chain C residue 30 type sequence P description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 13) chain C residue 40 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 14) chain C residue 41 type sequence G description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 15) chain C residue 48 type sequence Y description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 16) chain C residue 49 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 17) chain C residue 52 type sequence N description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 18) chain C residue 59 type sequence W description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 19) chain C residue 67 type sequence Y description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 20) chain C residue 78 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 21) chain C residue 79 type sequence K description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 22) chain C residue 80 type sequence M description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 23) chain C residue 81 type sequence I description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 24) chain C residue 82 type sequence F description binding site for Di-peptide HEC C 201 and CYS C 17 source : AC7 25) chain C residue 10 type sequence F description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 26) chain C residue 13 type sequence K description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 27) chain C residue 15 type sequence A description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 28) chain C residue 16 type sequence Q description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 29) chain C residue 17 type sequence C description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 30) chain C residue 18 type sequence H description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 31) chain C residue 28 type sequence E description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 32) chain C residue 29 type sequence G description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 33) chain C residue 30 type sequence P description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 34) chain C residue 40 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 35) chain C residue 41 type sequence G description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 36) chain C residue 48 type sequence Y description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 37) chain C residue 49 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 38) chain C residue 52 type sequence N description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 39) chain C residue 59 type sequence W description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 40) chain C residue 67 type sequence Y description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 41) chain C residue 78 type sequence T description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 42) chain C residue 79 type sequence K description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 43) chain C residue 80 type sequence M description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 44) chain C residue 81 type sequence I description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 45) chain C residue 82 type sequence F description binding site for Di-peptide HEC C 201 and CYS C 14 source : AC8 46) chain C residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:191069 source Swiss-Prot : SWS_FT_FI3 47) chain C residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI4 48) chain C residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI4 49) chain C residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI5 50) chain C residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 51) chain C residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 52) chain C residue 14 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 53) chain C residue 17 type BINDING sequence C description covalent source Swiss-Prot : SWS_FT_FI1 54) chain C residue 18 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI2 55) chain C residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI2

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