eF-site ID 1bfr-O PDB Code 1bfr Chain O click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence O:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain O residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MO 2) chain O residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MO 3) chain O residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MO 4) chain O residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MO 5) chain O residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MO 6) chain O residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MO 7) chain O residue 25 type sequence Y description BINDING SITE FOR RESIDUE MN O 201 source : DC2 8) chain O residue 51 type sequence E description BINDING SITE FOR RESIDUE MN O 201 source : DC2 9) chain O residue 94 type sequence E description BINDING SITE FOR RESIDUE MN O 201 source : DC2 10) chain O residue 127 type sequence E description BINDING SITE FOR RESIDUE MN O 201 source : DC2 11) chain O residue 130 type sequence H description BINDING SITE FOR RESIDUE MN O 201 source : DC2 12) chain O residue 18 type sequence E description BINDING SITE FOR RESIDUE MN O 202 source : DC3 13) chain O residue 51 type sequence E description BINDING SITE FOR RESIDUE MN O 202 source : DC3 14) chain O residue 54 type sequence H description BINDING SITE FOR RESIDUE MN O 202 source : DC3 15) chain O residue 127 type sequence E description BINDING SITE FOR RESIDUE MN O 202 source : DC3 16) chain O residue 23 type sequence N description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 17) chain O residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 18) chain O residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 19) chain O residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 20) chain O residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 21) chain O residue 55 type sequence A description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 22) chain O residue 56 type sequence D description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 23) chain O residue 18 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 24) chain O residue 46 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 25) chain O residue 50 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 26) chain O residue 51 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 27) chain O residue 54 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 28) chain O residue 94 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 29) chain O residue 127 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 30) chain O residue 130 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 31) chain O residue 52 type BINDING sequence M description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI2

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