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1I0R

CRYSTAL STRUCTURE OF FERRIC REDUCTASE FROM ARCHAEOGLOBUS FULGIDUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016723molecular_functionoxidoreductase activity, acting on metal ions, NAD or NADP as acceptor
A0042602molecular_functionriboflavin reductase (NADPH) activity
A0042803molecular_functionprotein homodimerization activity
A0052851molecular_functionferric-chelate reductase (NADPH) activity
A0140618molecular_functionferric-chelate reductase (NADH) activity
B0000166molecular_functionnucleotide binding
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016723molecular_functionoxidoreductase activity, acting on metal ions, NAD or NADP as acceptor
B0042602molecular_functionriboflavin reductase (NADPH) activity
B0042803molecular_functionprotein homodimerization activity
B0052851molecular_functionferric-chelate reductase (NADPH) activity
B0140618molecular_functionferric-chelate reductase (NADH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN A 2000
ChainResidue
AGLY26
AASN50
AASP51
ATHR52
AGLY80
APHE81
AARG82
ALYS83
ASER84
ALYS89
ATYR150
AGLN27
AHOH2028
AHOH2045
AHOH2101
AHOH2110
AILE28
AALA29
AASN30
ATHR31
ACYS45
ALEU46
AASN47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11525168","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I0S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11525168","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I0R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1I0S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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