5EXE
Crystal structure of oxalate oxidoreductase from Moorella thermoacetica bound with carboxy-TPP adduct
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
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 | 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 | 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 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0003824 | molecular_function | catalytic activity |
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 | 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 | 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 | 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 | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P94692 |
Chain | Residue | Details |
E | CYS261 | |
E | CYS264 | |
E | CYS267 | |
E | CYS271 | |
E | CYS290 | |
E | CYS293 | |
E | CYS296 | |
E | CYS300 | |
C | CYS24 | |
C | CYS27 | |
C | CYS52 | |
C | CYS225 | |
F | CYS24 | |
F | CYS27 | |
F | CYS52 | |
F | CYS225 |