eF-site ID 3zoo-ABCD PDB Code 3zoo Chain A, B, C, D click to enlarge Title Structure of the Y46F mutant of human cytochrome c Classification OXIDOREDUCTASE Compound CYTOCHROME C Source Homo sapiens (Human) (CYC_HUMAN) Sequence A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE B:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE C:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKKATNE D:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGFSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM 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 30 type sequence P description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 7) chain A residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 8) chain A residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 9) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 10) chain A residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 11) chain A residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 12) chain A residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 13) chain A residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 14) chain A residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 15) chain A residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 16) chain A residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 17) chain A residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 18) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 19) chain B residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC A 105 source : AC1 20) chain B residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 21) chain B residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 22) chain B residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 23) chain B residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 24) chain B residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 25) chain B residue 29 type sequence G description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 26) chain B residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 27) chain B residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 28) chain B residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 29) chain B residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 30) chain B residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 31) chain B residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 32) chain B residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 33) chain B residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 34) chain B residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 35) chain B residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 36) chain B residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 37) chain B residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC B 105 source : AC2 38) chain C residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 39) chain C residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 40) chain C residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 41) chain C residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 42) chain C residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 43) chain C residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 44) chain C residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 45) chain C residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 46) chain C residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 47) chain C residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 48) chain C residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 49) chain C residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 50) chain C residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 51) chain C residue 68 type sequence L description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 52) chain C residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 53) chain C residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 54) chain C residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 55) chain C residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 56) chain D residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC C 105 source : AC3 57) chain A residue 55 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 58) chain D residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 59) chain D residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 60) chain D residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 61) chain D residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 62) chain D residue 28 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 63) chain D residue 30 type sequence P description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 64) chain D residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 65) chain D residue 41 type sequence G description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 66) chain D residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 67) chain D residue 49 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 68) chain D residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 69) chain D residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 70) chain D residue 67 type sequence Y description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 71) chain D residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 72) chain D residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 73) chain D residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 74) chain D residue 81 type sequence I description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 75) chain D residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 76) chain D residue 85 type sequence I description BINDING SITE FOR RESIDUE HEC D 105 source : AC4 77) chain A residue 87 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1105 source : AC5 78) chain A residue 88 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1105 source : AC5 79) chain D residue 79 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1105 source : AC5 80) chain A residue 13 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1106 source : AC6 81) chain B residue 73 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1106 source : AC6 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) chain A residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 95) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 96) chain C residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 97) chain D residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 98) chain A residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 99) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 100) chain C residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 101) chain D residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 102) chain A residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 103) chain A residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 104) chain B residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 105) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 106) chain C residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 107) chain C residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 108) chain D residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 109) chain D residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 110) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 111) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 112) chain C residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 113) chain D residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 114) chain A residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 115) chain B residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 116) chain C residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 117) chain D residue 72 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 118) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 119) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 120) chain C residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 121) chain D residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8

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