eF-site ID 1bfr-P PDB Code 1bfr Chain P click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence P:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain P residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MP 2) chain P residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MP 3) chain P residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MP 4) chain P residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MP 5) chain P residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MP 6) chain P residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MP 7) chain P residue 51 type sequence E description BINDING SITE FOR RESIDUE MN P 201 source : DC4 8) chain P residue 94 type sequence E description BINDING SITE FOR RESIDUE MN P 201 source : DC4 9) chain P residue 127 type sequence E description BINDING SITE FOR RESIDUE MN P 201 source : DC4 10) chain P residue 130 type sequence H description BINDING SITE FOR RESIDUE MN P 201 source : DC4 11) chain P residue 18 type sequence E description BINDING SITE FOR RESIDUE MN P 202 source : DC5 12) chain P residue 51 type sequence E description BINDING SITE FOR RESIDUE MN P 202 source : DC5 13) chain P residue 54 type sequence H description BINDING SITE FOR RESIDUE MN P 202 source : DC5 14) chain P residue 127 type sequence E description BINDING SITE FOR RESIDUE MN P 202 source : DC5 15) chain P residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 16) chain P residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 17) chain P residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 18) chain P residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM P 200 source : GC2 19) chain P 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 P 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 P 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 P 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 P 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 P 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 P 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 P 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 P 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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