eF-site ID 1bfr-K PDB Code 1bfr Chain K click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence K:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain K residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MK 2) chain K residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MK 3) chain K residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MK 4) chain K residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MK 5) chain K residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MK 6) chain K residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MK 7) chain K residue 25 type sequence Y description BINDING SITE FOR RESIDUE MN K 201 source : CC3 8) chain K residue 51 type sequence E description BINDING SITE FOR RESIDUE MN K 201 source : CC3 9) chain K residue 94 type sequence E description BINDING SITE FOR RESIDUE MN K 201 source : CC3 10) chain K residue 127 type sequence E description BINDING SITE FOR RESIDUE MN K 201 source : CC3 11) chain K residue 130 type sequence H description BINDING SITE FOR RESIDUE MN K 201 source : CC3 12) chain K residue 18 type sequence E description BINDING SITE FOR RESIDUE MN K 202 source : CC4 13) chain K residue 51 type sequence E description BINDING SITE FOR RESIDUE MN K 202 source : CC4 14) chain K residue 54 type sequence H description BINDING SITE FOR RESIDUE MN K 202 source : CC4 15) chain K residue 127 type sequence E description BINDING SITE FOR RESIDUE MN K 202 source : CC4 16) chain K residue 23 type sequence N description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 17) chain K residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 18) chain K residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 19) chain K residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 20) chain K residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 21) chain K residue 55 type sequence A description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 22) chain K residue 56 type sequence D description BINDING SITE FOR RESIDUE HEM L 200 source : FC9 23) chain K 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 K 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 K 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 K 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 K 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 K 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 K 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 K 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 K 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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