1YCG
X-ray Structures of Moorella thermoacetica FprA. Novel Diiron Site Structure and Mechanistic Insights into a Scavenging Nitric Oxide Reductase
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | SER2 |
| A | GLU60 |
| C | HIS271 |
| C | ASP275 |
| C | ZN422 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| C | ZN421 |
| A | HIS271 |
| A | ASP275 |
| C | SER2 |
| C | GLU60 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HIS118 |
| A | HOH729 |
| D | GLU388 |
| D | HOH761 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 404 |
| Chain | Residue |
| A | GLU59 |
| A | HOH730 |
| A | HOH731 |
| A | HOH732 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 411 |
| Chain | Residue |
| B | SER2 |
| B | GLU60 |
| D | HIS271 |
| D | ASP275 |
| D | ZN432 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 412 |
| Chain | Residue |
| B | HIS271 |
| B | ASP275 |
| D | SER2 |
| D | GLU60 |
| D | ZN431 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 413 |
| Chain | Residue |
| B | ASP120 |
| B | HOH731 |
| B | HOH732 |
| B | HOH733 |
| B | HOH734 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 414 |
| Chain | Residue |
| B | GLU55 |
| B | GLU59 |
| B | HOH735 |
| B | HOH736 |
| B | HOH737 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 421 |
| Chain | Residue |
| A | HIS271 |
| A | ASP275 |
| A | ZN402 |
| C | SER2 |
| C | GLU60 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 422 |
| Chain | Residue |
| A | SER2 |
| A | GLU60 |
| A | ZN401 |
| C | HIS271 |
| C | ASP275 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN C 423 |
| Chain | Residue |
| C | PRO56 |
| C | GLU59 |
| C | HOH728 |
| C | HOH758 |
| C | HOH759 |
| C | HOH760 |
| C | HOH761 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 431 |
| Chain | Residue |
| B | HIS271 |
| B | ASP275 |
| B | ZN412 |
| D | SER2 |
| D | GLU60 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 432 |
| Chain | Residue |
| B | SER2 |
| B | GLU60 |
| B | ZN411 |
| D | HIS271 |
| D | ASP275 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 433 |
| Chain | Residue |
| D | GLU55 |
| D | HOH763 |
| D | HOH764 |
| D | HOH765 |
| D | HOH766 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO A 501 |
| Chain | Residue |
| A | HIS81 |
| A | GLU83 |
| A | ASP85 |
| A | HIS86 |
| A | HIS148 |
| A | ASP167 |
| A | HIS228 |
| A | EDO602 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 602 |
| Chain | Residue |
| A | PHE24 |
| A | HIS25 |
| A | GLU83 |
| A | ASP85 |
| A | HIS148 |
| A | ASP167 |
| A | HIS228 |
| A | FEO501 |
| site_id | BC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 701 |
| Chain | Residue |
| A | GLY346 |
| A | TRP347 |
| A | GLY348 |
| A | GLY349 |
| A | TRP376 |
| A | HOH715 |
| A | HOH716 |
| B | HIS25 |
| B | GLU83 |
| B | HIS148 |
| B | TRP149 |
| A | THR261 |
| A | MET262 |
| A | TRP263 |
| A | LEU264 |
| A | SER265 |
| A | THR266 |
| A | PRO312 |
| A | THR313 |
| A | ILE314 |
| A | ASN315 |
| A | ASN316 |
| A | ALA344 |
| A | TYR345 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO B 511 |
| Chain | Residue |
| B | HIS81 |
| B | GLU83 |
| B | ASP85 |
| B | HIS86 |
| B | HIS148 |
| B | ASP167 |
| B | HIS228 |
| B | EDO612 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 612 |
| Chain | Residue |
| B | PHE24 |
| B | HIS25 |
| B | GLU83 |
| B | ASP85 |
| B | HIS148 |
| B | ASP167 |
| B | HIS228 |
| B | FEO511 |
| site_id | CC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 711 |
| Chain | Residue |
| A | HIS25 |
| A | GLU83 |
| A | HIS148 |
| A | TRP149 |
| A | HOH728 |
| B | THR261 |
| B | MET262 |
| B | TRP263 |
| B | LEU264 |
| B | SER265 |
| B | THR266 |
| B | PRO312 |
| B | THR313 |
| B | ILE314 |
| B | ASN315 |
| B | ASN316 |
| B | ALA344 |
| B | TYR345 |
| B | GLY346 |
| B | TRP347 |
| B | GLY348 |
| B | GLY349 |
| B | TRP376 |
| B | HOH730 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO C 521 |
| Chain | Residue |
| C | HIS81 |
| C | GLU83 |
| C | ASP85 |
| C | HIS86 |
| C | HIS148 |
| C | ASP167 |
| C | HIS228 |
| C | EDO622 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 622 |
| Chain | Residue |
| C | PHE24 |
| C | HIS25 |
| C | GLU83 |
| C | ASP85 |
| C | HIS148 |
| C | FEO521 |
| site_id | CC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN C 721 |
| Chain | Residue |
| C | THR261 |
| C | MET262 |
| C | TRP263 |
| 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 | HOH748 |
| D | HIS25 |
| D | GLU83 |
| D | HIS148 |
| D | TRP149 |
| D | HOH758 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO D 531 |
| Chain | Residue |
| D | HIS81 |
| D | GLU83 |
| D | ASP85 |
| D | HIS86 |
| D | HIS148 |
| D | ASP167 |
| D | HIS228 |
| D | EDO632 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 632 |
| Chain | Residue |
| C | TRP263 |
| D | PHE24 |
| D | HIS25 |
| D | GLU83 |
| D | ASP85 |
| D | HIS148 |
| D | HIS228 |
| D | FEO531 |
| site_id | CC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN D 731 |
| Chain | Residue |
| C | HIS25 |
| C | GLU83 |
| C | HIS148 |
| C | TRP149 |
| D | THR261 |
| D | MET262 |
| D | TRP263 |
| D | LEU264 |
| D | SER265 |
| D | THR266 |
| D | PRO312 |
| D | THR313 |
| D | ILE314 |
| D | ASN315 |
| D | ASN316 |
| D | ALA344 |
| D | TYR345 |
| D | GLY346 |
| D | TRP347 |
| D | GLY348 |
| D | GLY349 |
| D | TRP376 |
| D | HOH759 |
| D | HOH760 |
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 | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP85 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP85 | |
| B | ASN198 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| C | ASP85 | |
| C | ASN198 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| D | ASP85 | |
| D | ASN198 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP85 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| C | ASP85 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| D | ASP85 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | TYR195 | |
| A | HIS25 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | TYR195 | |
| B | HIS25 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| C | TYR195 | |
| C | HIS25 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| D | TYR195 | |
| D | HIS25 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP85 | |
| A | ASN198 |
| 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 |
