eF-site ID 3zcf-ABCD PDB Code 3zcf Chain A, B, C, D click to enlarge Title Structure of recombinant human cytochrome c Classification ELECTRON TRANSPORT Compound CYTOCHROME C Source null (CYC_HUMAN) Sequence A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE B:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE C:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE D:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain A residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 2) chain A residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 3) chain A residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 4) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 5) chain A residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 6) chain A residue 29 type sequence G description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 7) chain A residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 8) chain A residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 9) chain A residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 10) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 11) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 12) chain A residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 13) chain A residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 14) chain A residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 15) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 16) chain A residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 17) chain A residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 18) chain A residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 19) chain A residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 20) chain A residue 81 type sequence I description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 21) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 22) chain A residue 85 type sequence I description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 23) chain B residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 24) chain B residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 25) chain B residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 26) chain B residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 27) chain B residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 28) chain B residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 29) chain B residue 29 type sequence G description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 30) chain B residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 31) chain B residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 32) chain B residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 33) chain B residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 34) chain B residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 35) chain B residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 36) chain B residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 37) chain B residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 38) chain B residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 39) chain B residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 40) chain B residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 41) chain B residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 42) chain B residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 43) chain B residue 94 type sequence L description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 44) chain C residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 45) chain C residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 46) chain C residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 47) chain C residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 48) chain C residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 49) chain C residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 50) chain C residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 51) chain C residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 52) chain C residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 53) chain C residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 54) chain C residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 55) chain C residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 56) chain C residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 57) chain C residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 58) chain C residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 59) chain C residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 60) chain C residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 61) chain C residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 62) chain C residue 94 type sequence L description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 63) chain D residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 64) chain A residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 65) chain D residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 66) chain D residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 67) chain D residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 68) chain D residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 69) chain D residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 70) chain D residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 71) chain D residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 72) chain D residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 73) chain D residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 74) chain D residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 75) chain D residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 76) chain D residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 77) chain D residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 78) chain D residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 79) chain D residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 80) chain D residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 81) chain D residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 82) chain D residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 83) chain D residue 85 type sequence I description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 84) chain D residue 94 type sequence L description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 85) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 86) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 87) chain C residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 88) chain D residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 89) chain A residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 90) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 91) chain C residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 92) chain D residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 93) chain C residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 94) chain C residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 95) chain D residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 96) chain D residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 97) chain A residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 98) chain A residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 99) chain B residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 100) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 101) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 102) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 103) chain C residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 104) chain D residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 105) chain A residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 106) chain B residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 107) chain C residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 108) chain D residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 109) 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 110) chain C residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 111) chain C residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 112) chain D residue 14 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 113) chain D residue 17 type BINDING sequence C description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584 source Swiss-Prot : SWS_FT_FI1 114) 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 115) 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 116) 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 117) 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 118) 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 119) chain C 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 120) chain D 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 121) chain A residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 122) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 123) chain C residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 124) chain D residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3

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