eF-site ID 1bfr-A PDB Code 1bfr Chain A click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence A:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain A residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MA 2) chain A residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MA 3) chain A residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MA 4) chain A residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MA 5) chain A residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MA 6) chain A residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MA 7) chain A residue 25 type sequence Y description BINDING SITE FOR RESIDUE MN A 201 source : AC1 8) chain A residue 51 type sequence E description BINDING SITE FOR RESIDUE MN A 201 source : AC1 9) chain A residue 94 type sequence E description BINDING SITE FOR RESIDUE MN A 201 source : AC1 10) chain A residue 127 type sequence E description BINDING SITE FOR RESIDUE MN A 201 source : AC1 11) chain A residue 130 type sequence H description BINDING SITE FOR RESIDUE MN A 201 source : AC1 12) chain A residue 18 type sequence E description BINDING SITE FOR RESIDUE MN A 202 source : AC2 13) chain A residue 51 type sequence E description BINDING SITE FOR RESIDUE MN A 202 source : AC2 14) chain A residue 54 type sequence H description BINDING SITE FOR RESIDUE MN A 202 source : AC2 15) chain A residue 127 type sequence E description BINDING SITE FOR RESIDUE MN A 202 source : AC2 16) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 17) chain A residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 18) chain A residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 19) chain A residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 20) chain A residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 21) chain A residue 55 type sequence A description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 22) chain A residue 56 type sequence D description BINDING SITE FOR RESIDUE HEM B 200 source : FC4 23) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 50 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 51 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 54 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 94 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 127 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 130 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 18 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00085, ECO:0000269|PubMed:17077480 source Swiss-Prot : SWS_FT_FI1 31) chain A 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 32) chain A residue 1-19 type prosite sequence MKGDTKVINYLNKLLGNEL description BACTERIOFERRITIN Bacterioferritin signature. MkGdtkVInyLnklLgneL source prosite : PS00549

Display surface Download Links