eF-site ID 1bfr-X PDB Code 1bfr Chain X click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence X:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain X residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MX 2) chain X residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MX 3) chain X residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MX 4) chain X residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MX 5) chain X residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MX 6) chain X residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MX 7) chain X residue 51 type sequence E description BINDING SITE FOR RESIDUE MN X 201 source : FC2 8) chain X residue 94 type sequence E description BINDING SITE FOR RESIDUE MN X 201 source : FC2 9) chain X residue 127 type sequence E description BINDING SITE FOR RESIDUE MN X 201 source : FC2 10) chain X residue 130 type sequence H description BINDING SITE FOR RESIDUE MN X 201 source : FC2 11) chain X residue 18 type sequence E description BINDING SITE FOR RESIDUE MN X 202 source : FC3 12) chain X residue 51 type sequence E description BINDING SITE FOR RESIDUE MN X 202 source : FC3 13) chain X residue 54 type sequence H description BINDING SITE FOR RESIDUE MN X 202 source : FC3 14) chain X residue 127 type sequence E description BINDING SITE FOR RESIDUE MN X 202 source : FC3 15) chain X residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 16) chain X residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 17) chain X residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 18) chain X residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 19) chain X residue 18 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 20) chain X residue 46 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 21) chain X residue 50 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 22) chain X residue 51 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 23) chain X residue 54 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 24) chain X residue 94 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 25) chain X residue 127 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 26) chain X residue 130 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 27) chain X 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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