5EXE
Crystal structure of oxalate oxidoreductase from Moorella thermoacetica bound with carboxy-TPP adduct
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| A | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0033611 | biological_process | oxalate catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| B | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| B | 0033611 | biological_process | oxalate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0033611 | biological_process | oxalate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| D | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0033611 | biological_process | oxalate catabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| E | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| E | 0033611 | biological_process | oxalate catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| F | 0030976 | molecular_function | thiamine pyrophosphate binding |
| F | 0033611 | biological_process | oxalate catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 401 |
| Chain | Residue |
| B | CYS271 |
| B | CYS290 |
| B | LYS291 |
| B | GLY292 |
| B | CYS293 |
| B | GLY294 |
| B | CYS296 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 B 402 |
| Chain | Residue |
| B | THR262 |
| B | CYS264 |
| B | TYR265 |
| B | CYS267 |
| B | CYS300 |
| B | SER302 |
| B | LEU305 |
| B | ILE256 |
| B | CYS261 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 C 401 |
| Chain | Residue |
| B | ARG58 |
| C | CYS24 |
| C | CYS27 |
| C | PRO29 |
| C | CYS52 |
| C | ASN138 |
| C | CYS225 |
| C | PRO226 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue 5SR C 402 |
| Chain | Residue |
| A | TYR28 |
| A | PRO29 |
| A | ILE30 |
| A | GLU59 |
| A | VAL83 |
| A | ARG109 |
| A | ASP116 |
| A | PHE117 |
| C | THR50 |
| C | GLY51 |
| C | CYS52 |
| C | VAL55 |
| C | ILE74 |
| C | GLY109 |
| C | ASP110 |
| C | GLY111 |
| C | GLY112 |
| C | TYR136 |
| C | ASN138 |
| C | SER140 |
| C | TYR141 |
| C | ALA142 |
| C | ASN143 |
| C | THR144 |
| C | MG403 |
| C | HOH516 |
| C | HOH526 |
| C | HOH608 |
| C | HOH676 |
| D | GLU90 |
| D | HOH521 |
| D | HOH522 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| C | ASP110 |
| C | ASN138 |
| C | SER140 |
| C | 5SR402 |
| C | HOH608 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 404 |
| Chain | Residue |
| C | ASP130 |
| C | LEU211 |
| C | GLN213 |
| C | HOH562 |
| C | HOH566 |
| C | HOH707 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 E 401 |
| Chain | Residue |
| E | CYS271 |
| E | PHE285 |
| E | CYS290 |
| E | LYS291 |
| E | GLY292 |
| E | CYS293 |
| E | GLY294 |
| E | CYS296 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 E 402 |
| Chain | Residue |
| E | CYS261 |
| E | THR262 |
| E | GLU263 |
| E | CYS264 |
| E | TYR265 |
| E | CYS267 |
| E | CYS300 |
| E | PRO301 |
| E | LEU305 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 F 401 |
| Chain | Residue |
| E | ARG58 |
| F | CYS24 |
| F | CYS27 |
| F | PRO29 |
| F | CYS52 |
| F | ASN138 |
| F | CYS225 |
| F | PRO226 |
| site_id | AD1 |
| Number of Residues | 28 |
| Details | binding site for residue 5SR F 402 |
| Chain | Residue |
| D | HOH433 |
| F | THR50 |
| F | GLY51 |
| F | CYS52 |
| F | ILE74 |
| F | GLY109 |
| F | ASP110 |
| F | GLY111 |
| F | GLY112 |
| F | TYR136 |
| F | ASN138 |
| F | SER140 |
| F | TYR141 |
| F | ALA142 |
| F | ASN143 |
| F | THR144 |
| F | MG403 |
| F | HOH517 |
| F | HOH574 |
| F | HOH628 |
| F | HOH690 |
| D | PRO29 |
| D | ILE30 |
| D | GLU59 |
| D | VAL83 |
| D | ARG109 |
| D | ASP116 |
| D | PHE117 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG F 403 |
| Chain | Residue |
| F | ASP110 |
| F | ASN138 |
| F | SER140 |
| F | 5SR402 |
| F | HOH628 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA F 404 |
| Chain | Residue |
| F | ASP130 |
| F | LEU211 |
| F | GLN213 |
| F | HOH541 |
| F | HOH627 |
| F | HOH728 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CtECYtCWiYCP |
| Chain | Residue | Details |
| B | CYS261-PRO272 | |
| B | CYS290-PRO301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P94692","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
