1YCF
Oxidized (di-ferric) FprA from Moorella thermoacetica
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | SER2 |
| A | GLU60 |
| C | HIS271 |
| C | ASP275 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | HIS271 |
| A | ASP275 |
| C | SER2 |
| C | GLU60 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 512 |
| Chain | Residue |
| D | HIS271 |
| B | VAL17 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO A 500 |
| Chain | Residue |
| A | HIS81 |
| A | GLU83 |
| A | ASP85 |
| A | HIS86 |
| A | HIS148 |
| A | ASP167 |
| A | HIS228 |
| A | OXY501 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXY A 501 |
| Chain | Residue |
| A | PHE24 |
| A | HIS25 |
| A | GLU83 |
| A | TYR195 |
| A | ILE199 |
| A | FEO500 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN A 701 |
| Chain | Residue |
| A | THR261 |
| A | MET262 |
| A | TRP263 |
| A | LEU264 |
| A | SER265 |
| A | THR266 |
| A | PRO312 |
| A | THR313 |
| A | ILE314 |
| A | ASN315 |
| A | ASN316 |
| A | TYR345 |
| A | GLY346 |
| A | TRP347 |
| A | GLY348 |
| A | GLY349 |
| A | TRP376 |
| A | HOH623 |
| B | HIS25 |
| B | GLU83 |
| B | TRP149 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FEO B 510 |
| Chain | Residue |
| B | HIS25 |
| B | HIS81 |
| B | GLU83 |
| B | ASP85 |
| B | HIS86 |
| B | HIS148 |
| B | ASP167 |
| B | HIS228 |
| B | OXY511 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OXY B 511 |
| Chain | Residue |
| B | PHE24 |
| B | HIS25 |
| B | ASP167 |
| B | TYR195 |
| B | HIS228 |
| B | FEO510 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN B 702 |
| Chain | Residue |
| A | HIS25 |
| A | GLU83 |
| A | TRP149 |
| B | THR261 |
| B | MET262 |
| B | TRP263 |
| B | LEU264 |
| B | SER265 |
| B | THR266 |
| B | PRO312 |
| B | THR313 |
| B | ILE314 |
| B | ASN315 |
| B | ASN316 |
| B | TYR345 |
| B | GLY346 |
| B | TRP347 |
| B | GLY348 |
| B | GLY349 |
| B | TRP376 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO C 520 |
| Chain | Residue |
| C | HIS81 |
| C | GLU83 |
| C | ASP85 |
| C | HIS86 |
| C | HIS148 |
| C | ASP167 |
| C | HIS228 |
| C | OXY521 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXY C 521 |
| Chain | Residue |
| C | PHE24 |
| C | HIS25 |
| C | GLU83 |
| C | HIS148 |
| C | ASP167 |
| C | TYR195 |
| C | ILE199 |
| C | FEO520 |
| site_id | BC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN C 703 |
| Chain | Residue |
| C | LEU264 |
| C | SER265 |
| C | THR266 |
| C | PRO312 |
| C | THR313 |
| C | ILE314 |
| C | ASN315 |
| C | ASN316 |
| C | ALA344 |
| C | TYR345 |
| C | GLY346 |
| C | TRP347 |
| C | GLY348 |
| C | GLY349 |
| C | TRP376 |
| C | HOH650 |
| D | HIS25 |
| D | GLU83 |
| D | TRP149 |
| C | THR261 |
| C | MET262 |
| C | TRP263 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO D 530 |
| Chain | Residue |
| D | HIS81 |
| D | GLU83 |
| D | ASP85 |
| D | HIS86 |
| D | HIS148 |
| D | ASP167 |
| D | HIS228 |
| D | OXY531 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXY D 531 |
| Chain | Residue |
| D | PHE24 |
| D | HIS25 |
| D | GLU83 |
| D | HIS148 |
| D | ASP167 |
| D | TYR195 |
| D | HIS228 |
| D | FEO530 |
| site_id | BC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN D 704 |
| Chain | Residue |
| C | HIS25 |
| C | GLU83 |
| C | TRP149 |
| D | THR261 |
| D | MET262 |
| D | TRP263 |
| D | LEU264 |
| D | SER265 |
| D | THR266 |
| D | PRO312 |
| D | THR313 |
| D | ASN315 |
| D | ASN316 |
| D | ALA344 |
| D | TYR345 |
| D | GLY346 |
| D | TRP347 |
| D | GLY348 |
| D | GLY349 |
| D | TRP376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 556 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 756 |
| Details | Region: {"description":"Zinc metallo-hydrolase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15850383 |
| Chain | Residue | Details |
| A | TYR195 | |
| A | HIS25 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15850383 |
| Chain | Residue | Details |
| B | TYR195 | |
| B | HIS25 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15850383 |
| Chain | Residue | Details |
| C | TYR195 | |
| C | HIS25 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15850383 |
| Chain | Residue | Details |
| D | TYR195 | |
| D | HIS25 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 497 |
| Chain | Residue | Details |
| A | HIS25 | proton shuttle (general acid/base) |
| A | HIS81 | metal ligand |
| A | GLU83 | metal ligand |
| A | ASP85 | metal ligand |
| A | HIS148 | metal ligand |
| A | ASP167 | metal ligand |
| A | TYR195 | proton shuttle (general acid/base) |
| A | HIS228 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 497 |
| Chain | Residue | Details |
| B | HIS25 | proton shuttle (general acid/base) |
| B | HIS81 | metal ligand |
| B | GLU83 | metal ligand |
| B | ASP85 | metal ligand |
| B | HIS148 | metal ligand |
| B | ASP167 | metal ligand |
| B | TYR195 | proton shuttle (general acid/base) |
| B | HIS228 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 497 |
| Chain | Residue | Details |
| C | HIS25 | proton shuttle (general acid/base) |
| C | HIS81 | metal ligand |
| C | GLU83 | metal ligand |
| C | ASP85 | metal ligand |
| C | HIS148 | metal ligand |
| C | ASP167 | metal ligand |
| C | TYR195 | proton shuttle (general acid/base) |
| C | HIS228 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 497 |
| Chain | Residue | Details |
| D | HIS25 | proton shuttle (general acid/base) |
| D | HIS81 | metal ligand |
| D | GLU83 | metal ligand |
| D | ASP85 | metal ligand |
| D | HIS148 | metal ligand |
| D | ASP167 | metal ligand |
| D | TYR195 | proton shuttle (general acid/base) |
| D | HIS228 | metal ligand |
