eF-site ID 1bfr-W PDB Code 1bfr Chain W click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence W:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain W residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MW 2) chain W residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MW 3) chain W residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MW 4) chain W residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MW 5) chain W residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MW 6) chain W residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MW 7) chain W residue 25 type sequence Y description BINDING SITE FOR RESIDUE MN W 201 source : EC9 8) chain W residue 51 type sequence E description BINDING SITE FOR RESIDUE MN W 201 source : EC9 9) chain W residue 94 type sequence E description BINDING SITE FOR RESIDUE MN W 201 source : EC9 10) chain W residue 127 type sequence E description BINDING SITE FOR RESIDUE MN W 201 source : EC9 11) chain W residue 130 type sequence H description BINDING SITE FOR RESIDUE MN W 201 source : EC9 12) chain W residue 18 type sequence E description BINDING SITE FOR RESIDUE MN W 202 source : FC1 13) chain W residue 51 type sequence E description BINDING SITE FOR RESIDUE MN W 202 source : FC1 14) chain W residue 54 type sequence H description BINDING SITE FOR RESIDUE MN W 202 source : FC1 15) chain W residue 127 type sequence E description BINDING SITE FOR RESIDUE MN W 202 source : FC1 16) chain W residue 23 type sequence N description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 17) chain W residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 18) chain W residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 19) chain W residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 20) chain W residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 21) chain W residue 55 type sequence A description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 22) chain W residue 56 type sequence D description BINDING SITE FOR RESIDUE HEM X 200 source : GC6 23) chain W 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 W 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 W 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 W 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 W 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 W 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 W 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 W 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 W 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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