eF-site ID 5ty3-B PDB Code 5ty3 Chain B click to enlarge Title Crystal structure of K72A variant of Human Cytochrome c Classification ELECTRON TRANSPORT Compound Cytochrome c Source Homo sapiens (Human) (CYC_HUMAN) Sequence B:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPAKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain B residue 55 type sequence K description binding site for residue HEC A 201 source : AC1 2) chain B residue 86 type sequence K description binding site for residue SO4 A 202 source : AC2 3) chain B residue 13 type sequence K description binding site for residue HEC B 201 source : AC3 4) chain B residue 18 type sequence H description binding site for residue HEC B 201 source : AC3 5) chain B residue 28 type sequence T description binding site for residue HEC B 201 source : AC3 6) chain B residue 29 type sequence G description binding site for residue HEC B 201 source : AC3 7) chain B residue 30 type sequence P description binding site for residue HEC B 201 source : AC3 8) chain B residue 40 type sequence T description binding site for residue HEC B 201 source : AC3 9) chain B residue 41 type sequence G description binding site for residue HEC B 201 source : AC3 10) chain B residue 46 type sequence Y description binding site for residue HEC B 201 source : AC3 11) chain B residue 48 type sequence Y description binding site for residue HEC B 201 source : AC3 12) chain B residue 49 type sequence T description binding site for residue HEC B 201 source : AC3 13) chain B residue 52 type sequence N description binding site for residue HEC B 201 source : AC3 14) chain B residue 59 type sequence W description binding site for residue HEC B 201 source : AC3 15) chain B residue 67 type sequence Y description binding site for residue HEC B 201 source : AC3 16) chain B residue 78 type sequence T description binding site for residue HEC B 201 source : AC3 17) chain B residue 79 type sequence K description binding site for residue HEC B 201 source : AC3 18) chain B residue 80 type sequence M description binding site for residue HEC B 201 source : AC3 19) chain B residue 81 type sequence I description binding site for residue HEC B 201 source : AC3 20) chain B residue 82 type sequence F description binding site for residue HEC B 201 source : AC3 21) chain B residue 36 type sequence F description binding site for residue SO4 B 202 source : AC4 22) chain B residue 60 type sequence G description binding site for residue SO4 B 202 source : AC4 23) chain B residue 61 type sequence E description binding site for residue SO4 B 202 source : AC4 24) chain B residue 99 type sequence K description binding site for residue SO4 B 202 source : AC4 25) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 26) 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 27) 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 28) 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 29) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 30) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 72 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7

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