eF-site ID 5ty3-AB PDB Code 5ty3 Chain A, 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 A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPAKYIPGTKM IFVGIKKKEERADLIAYLKKATNE B:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWGEDTLMEYLENPAKYIPGTKM IFVGIKKKEERADLIAYLKKATNE Description Functional site 1) chain A residue 13 type sequence K description binding site for residue HEC A 201 source : AC1 2) chain A residue 18 type sequence H description binding site for residue HEC A 201 source : AC1 3) chain A residue 28 type sequence T description binding site for residue HEC A 201 source : AC1 4) chain A residue 29 type sequence G description binding site for residue HEC A 201 source : AC1 5) chain A residue 30 type sequence P description binding site for residue HEC A 201 source : AC1 6) chain A residue 40 type sequence T description binding site for residue HEC A 201 source : AC1 7) chain A residue 41 type sequence G description binding site for residue HEC A 201 source : AC1 8) chain A residue 46 type sequence Y description binding site for residue HEC A 201 source : AC1 9) chain A residue 48 type sequence Y description binding site for residue HEC A 201 source : AC1 10) chain A residue 49 type sequence T description binding site for residue HEC A 201 source : AC1 11) chain A residue 52 type sequence N description binding site for residue HEC A 201 source : AC1 12) chain A residue 59 type sequence W description binding site for residue HEC A 201 source : AC1 13) chain A residue 67 type sequence Y description binding site for residue HEC A 201 source : AC1 14) chain A residue 78 type sequence T description binding site for residue HEC A 201 source : AC1 15) chain A residue 79 type sequence K description binding site for residue HEC A 201 source : AC1 16) chain A residue 80 type sequence M description binding site for residue HEC A 201 source : AC1 17) chain A residue 81 type sequence I description binding site for residue HEC A 201 source : AC1 18) chain A residue 82 type sequence F description binding site for residue HEC A 201 source : AC1 19) chain B residue 55 type sequence K description binding site for residue HEC A 201 source : AC1 20) chain A residue 49 type sequence T description binding site for residue SO4 A 202 source : AC2 21) chain A residue 50 type sequence A description binding site for residue SO4 A 202 source : AC2 22) chain B residue 86 type sequence K description binding site for residue SO4 A 202 source : AC2 23) chain B residue 13 type sequence K description binding site for residue HEC B 201 source : AC3 24) chain B residue 18 type sequence H description binding site for residue HEC B 201 source : AC3 25) chain B residue 28 type sequence T description binding site for residue HEC B 201 source : AC3 26) chain B residue 29 type sequence G description binding site for residue HEC B 201 source : AC3 27) chain B residue 30 type sequence P description binding site for residue HEC B 201 source : AC3 28) chain B residue 40 type sequence T description binding site for residue HEC B 201 source : AC3 29) chain B residue 41 type sequence G description binding site for residue HEC B 201 source : AC3 30) chain B residue 46 type sequence Y description binding site for residue HEC B 201 source : AC3 31) chain B residue 48 type sequence Y description binding site for residue HEC B 201 source : AC3 32) chain B residue 49 type sequence T description binding site for residue HEC B 201 source : AC3 33) chain B residue 52 type sequence N description binding site for residue HEC B 201 source : AC3 34) chain B residue 59 type sequence W description binding site for residue HEC B 201 source : AC3 35) chain B residue 67 type sequence Y description binding site for residue HEC B 201 source : AC3 36) chain B residue 78 type sequence T description binding site for residue HEC B 201 source : AC3 37) chain B residue 79 type sequence K description binding site for residue HEC B 201 source : AC3 38) chain B residue 80 type sequence M description binding site for residue HEC B 201 source : AC3 39) chain B residue 81 type sequence I description binding site for residue HEC B 201 source : AC3 40) chain B residue 82 type sequence F description binding site for residue HEC B 201 source : AC3 41) chain B residue 36 type sequence F description binding site for residue SO4 B 202 source : AC4 42) chain B residue 60 type sequence G description binding site for residue SO4 B 202 source : AC4 43) chain B residue 61 type sequence E description binding site for residue SO4 B 202 source : AC4 44) chain B residue 99 type sequence K description binding site for residue SO4 B 202 source : AC4 45) 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 46) 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 47) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 48) chain B residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI8 49) chain A residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 1 type MOD_RES sequence G description N-acetylglycine => ECO:0000269|PubMed:13933734 source Swiss-Prot : SWS_FT_FI4 51) chain A residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 52) chain A residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 53) chain B residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 54) chain B residue 97 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62894 source Swiss-Prot : SWS_FT_FI5 55) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 56) chain B residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI6 57) chain A residue 72 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 58) chain B residue 72 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897 source Swiss-Prot : SWS_FT_FI7 59) 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 60) 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 61) 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 62) 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 63) chain A residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3 64) chain B residue 80 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI3

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