eF-site ID 256b-AB PDB Code 256b Chain A, B click to enlarge Title IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS Classification ELECTRON TRANSPORT Compound CYTOCHROME B562 Source Escherichia coli (C562_ECOLI) Sequence A:  ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTRNAYHQKYR B:  ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTRNAYHQKYR Description Functional site 1) chain B residue 59 type sequence K description BINDING SITE FOR RESIDUE SO4 B 107 source : AC1 2) chain B residue 62 type sequence R description BINDING SITE FOR RESIDUE SO4 B 107 source : AC1 3) chain B residue 95 type sequence K description BINDING SITE FOR RESIDUE SO4 B 108 source : AC2 4) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE SO4 B 108 source : AC2 5) chain A residue 59 type sequence K description BINDING SITE FOR RESIDUE SO4 A 107 source : AC3 6) chain A residue 62 type sequence R description BINDING SITE FOR RESIDUE SO4 A 107 source : AC3 7) chain A residue 95 type sequence K description BINDING SITE FOR RESIDUE SO4 A 108 source : AC4 8) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE SO4 A 108 source : AC4 9) chain A residue 4 type sequence E description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 10) chain A residue 7 type sequence M description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 11) chain A residue 8 type sequence E description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 12) chain A residue 45 type sequence P description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 13) chain A residue 61 type sequence F description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 14) chain A residue 65 type sequence F description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 15) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 16) chain A residue 101 type sequence Y description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 17) chain A residue 102 type sequence H description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 18) chain A residue 105 type sequence Y description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 19) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE HEM A 109 source : AC5 20) chain B residue 4 type sequence E description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 21) chain B residue 7 type sequence M description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 22) chain B residue 46 type sequence P description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 23) chain B residue 61 type sequence F description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 24) chain B residue 65 type sequence F description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 25) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 26) chain B residue 101 type sequence Y description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 27) chain B residue 102 type sequence H description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 28) chain B residue 105 type sequence Y description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 29) chain B residue 106 type sequence R description BINDING SITE FOR RESIDUE HEM B 109 source : AC6 30) chain B residue 7 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI1 31) chain B residue 102 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI1 32) chain A residue 7 type BINDING sequence M description axial binding residue source Swiss-Prot : SWS_FT_FI1 33) chain A residue 102 type BINDING sequence H description axial binding residue source Swiss-Prot : SWS_FT_FI1

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