eF-site ID 1bfr-R PDB Code 1bfr Chain R click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence R:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain R residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MR 2) chain R residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MR 3) chain R residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MR 4) chain R residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MR 5) chain R residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MR 6) chain R residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MR 7) chain R residue 51 type sequence E description BINDING SITE FOR RESIDUE MN R 201 source : DC8 8) chain R residue 94 type sequence E description BINDING SITE FOR RESIDUE MN R 201 source : DC8 9) chain R residue 127 type sequence E description BINDING SITE FOR RESIDUE MN R 201 source : DC8 10) chain R residue 130 type sequence H description BINDING SITE FOR RESIDUE MN R 201 source : DC8 11) chain R residue 18 type sequence E description BINDING SITE FOR RESIDUE MN R 202 source : DC9 12) chain R residue 51 type sequence E description BINDING SITE FOR RESIDUE MN R 202 source : DC9 13) chain R residue 54 type sequence H description BINDING SITE FOR RESIDUE MN R 202 source : DC9 14) chain R residue 127 type sequence E description BINDING SITE FOR RESIDUE MN R 202 source : DC9 15) chain R residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 16) chain R residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 17) chain R residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 18) chain R residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 19) chain R 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 R 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 R 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 R 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 R 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 R 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 R 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 R 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 R 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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