eF-site ID 1cyc-AB PDB Code 1cyc Chain A, B click to enlarge Title THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION Classification ELECTRON TRANSPORT Compound FERROCYTOCHROME C Source null (CYC_KATPE) Sequence A:  GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKT GQAEGYSYTDANKSKGIVWNENTLMEYLENPKKYIPGTKM IFAGIKKKGERQDLVAYLKSATS B:  GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKT GQAEGYSYTDANKSKGIVWNENTLMEYLENPKKYIPGTKM IFAGIKKKGERQDLVAYLKSATS Description (1)  FERROCYTOCHROME C Functional site 1) chain A residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 2) chain A residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 3) chain A residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 4) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 5) chain A residue 32 type sequence L description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 6) chain A residue 35 type sequence L description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 7) chain A residue 38 type sequence R description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 8) chain A residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 9) chain A residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 10) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 11) chain A residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 12) chain A residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 13) chain A residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 14) chain A residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 15) chain A residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 16) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC A 104 source : AC1 17) chain B residue 13 type sequence K description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 18) chain B residue 14 type sequence C description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 19) chain B residue 17 type sequence C description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 20) chain B residue 18 type sequence H description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 21) chain B residue 32 type sequence L description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 22) chain B residue 35 type sequence L description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 23) chain B residue 38 type sequence R description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 24) chain B residue 40 type sequence T description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 25) chain B residue 46 type sequence Y description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 26) chain B residue 48 type sequence Y description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 27) chain B residue 52 type sequence N description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 28) chain B residue 59 type sequence W description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 29) chain B residue 78 type sequence T description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 30) chain B residue 79 type sequence K description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 31) chain B residue 80 type sequence M description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 32) chain B residue 82 type sequence F description BINDING SITE FOR RESIDUE HEC B 104 source : AC2 33) chain A residue 15 type BINDING sequence A description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 18 type BINDING sequence H description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 15 type BINDING sequence A description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 18 type BINDING sequence H description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 19 type BINDING sequence T description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 81 type BINDING sequence I description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 19 type BINDING sequence T description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 81 type BINDING sequence I description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 2 type MOD_RES sequence D description N-acetylglycine => ECO:0000269|PubMed:5106585 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 2 type MOD_RES sequence D description N-acetylglycine => ECO:0000269|PubMed:5106585 source Swiss-Prot : SWS_FT_FI3

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