eF-site ID 1bfr-Q PDB Code 1bfr Chain Q click to enlarge Title IRON STORAGE AND ELECTRON TRANSPORT Classification ELECTRON TRANSPORT Compound BACTERIOFERRITIN Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence Q:  MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRL NDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIG EDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMM IEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG Description Functional site 1) chain Q residue 18 type sequence E description BINUCLEAR METAL-BINDING SITE source : MQ 2) chain Q residue 51 type sequence E description BINUCLEAR METAL-BINDING SITE source : MQ 3) chain Q residue 54 type sequence H description BINUCLEAR METAL-BINDING SITE source : MQ 4) chain Q residue 94 type sequence E description BINUCLEAR METAL-BINDING SITE source : MQ 5) chain Q residue 127 type sequence E description BINUCLEAR METAL-BINDING SITE source : MQ 6) chain Q residue 130 type sequence H description BINUCLEAR METAL-BINDING SITE source : MQ 7) chain Q residue 25 type sequence Y description BINDING SITE FOR RESIDUE MN Q 201 source : DC6 8) chain Q residue 51 type sequence E description BINDING SITE FOR RESIDUE MN Q 201 source : DC6 9) chain Q residue 94 type sequence E description BINDING SITE FOR RESIDUE MN Q 201 source : DC6 10) chain Q residue 127 type sequence E description BINDING SITE FOR RESIDUE MN Q 201 source : DC6 11) chain Q residue 130 type sequence H description BINDING SITE FOR RESIDUE MN Q 201 source : DC6 12) chain Q residue 18 type sequence E description BINDING SITE FOR RESIDUE MN Q 202 source : DC7 13) chain Q residue 51 type sequence E description BINDING SITE FOR RESIDUE MN Q 202 source : DC7 14) chain Q residue 54 type sequence H description BINDING SITE FOR RESIDUE MN Q 202 source : DC7 15) chain Q residue 127 type sequence E description BINDING SITE FOR RESIDUE MN Q 202 source : DC7 16) chain Q residue 23 type sequence N description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 17) chain Q residue 26 type sequence F description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 18) chain Q residue 45 type sequence Y description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 19) chain Q residue 52 type sequence M description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 20) chain Q residue 53 type sequence K description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 21) chain Q residue 55 type sequence A description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 22) chain Q residue 56 type sequence D description BINDING SITE FOR RESIDUE HEM R 200 source : GC3 23) chain Q 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 Q 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 Q 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 Q 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 Q 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 Q 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 Q 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 Q 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 Q 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

Display surface Download Links