3P7X
Crystal structure of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC8325
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0008379 | molecular_function | thioredoxin peroxidase activity |
A | 0016209 | molecular_function | antioxidant activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016684 | molecular_function | oxidoreductase activity, acting on peroxide as acceptor |
A | 0098869 | biological_process | cellular oxidant detoxification |
A | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0008379 | molecular_function | thioredoxin peroxidase activity |
B | 0016209 | molecular_function | antioxidant activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016684 | molecular_function | oxidoreductase activity, acting on peroxide as acceptor |
B | 0098869 | biological_process | cellular oxidant detoxification |
B | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
C | 0004601 | molecular_function | peroxidase activity |
C | 0008379 | molecular_function | thioredoxin peroxidase activity |
C | 0016209 | molecular_function | antioxidant activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016684 | molecular_function | oxidoreductase activity, acting on peroxide as acceptor |
C | 0098869 | biological_process | cellular oxidant detoxification |
C | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0008379 | molecular_function | thioredoxin peroxidase activity |
D | 0016209 | molecular_function | antioxidant activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016684 | molecular_function | oxidoreductase activity, acting on peroxide as acceptor |
D | 0098869 | biological_process | cellular oxidant detoxification |
D | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 165 |
Chain | Residue |
A | THR2 |
A | GLU3 |
A | HIS12 |
A | LEU13 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 166 |
Chain | Residue |
A | ILE18 |
A | PHE23 |
B | ASP61 |
B | ARG65 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 167 |
Chain | Residue |
C | ASP61 |
C | ARG65 |
D | ILE18 |
D | ASP22 |
D | PHE23 |
A | GLY8 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 A 168 |
Chain | Residue |
A | LYS45 |
A | LYS73 |
A | GLU74 |
A | GLU75 |
A | ILE77 |
B | ASP99 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 169 |
Chain | Residue |
A | ASN35 |
A | ASP41 |
A | TYR42 |
A | HOH210 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DTV A 170 |
Chain | Residue |
A | ARG124 |
A | HOH287 |
A | HOH344 |
C | ARG124 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 B 165 |
Chain | Residue |
B | PHE6 |
B | LYS7 |
B | PG4167 |
D | PHE87 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 B 166 |
Chain | Residue |
B | LYS7 |
B | GLY8 |
D | PHE6 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 B 167 |
Chain | Residue |
B | THR57 |
B | GLY58 |
B | VAL59 |
B | CYS60 |
B | ARG128 |
B | PG4165 |
D | ARG91 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 165 |
Chain | Residue |
C | ALA71 |
C | SER72 |
C | LYS73 |
C | GLU74 |
C | PG4169 |
C | HOH190 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 C 166 |
Chain | Residue |
C | ALA43 |
C | GLY44 |
C | LYS45 |
C | LYS73 |
C | GLU74 |
C | GLU75 |
C | GLY76 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 C 167 |
Chain | Residue |
C | ASN35 |
C | VAL37 |
C | ASP41 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 C 168 |
Chain | Residue |
C | ASP31 |
C | ASP33 |
C | ASP99 |
C | HOH243 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 C 169 |
Chain | Residue |
C | SER69 |
C | ASP70 |
C | LYS162 |
C | SO4165 |
C | HOH184 |
D | ASP136 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 C 170 |
Chain | Residue |
A | GLY9 |
C | GLN62 |
C | LYS66 |
D | ASP22 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PG4 C 171 |
Chain | Residue |
A | GLY-1 |
A | SER0 |
A | MET1 |
A | GLY8 |
C | THR57 |
C | GLY58 |
C | VAL59 |
C | HOH418 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 C 172 |
Chain | Residue |
C | GLU20 |
C | TYR141 |
C | LYS142 |
C | ILE144 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 D 165 |
Chain | Residue |
B | LYS90 |
D | ASP56 |
D | GLY58 |
D | GLN62 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DTU D 166 |
Chain | Residue |
B | ARG124 |
D | ARG124 |
Functional Information from PROSITE/UniProt
site_id | PS01265 |
Number of Residues | 12 |
Details | TPX Tpx family signature. SaDLPFAqkRWC |
Chain | Residue | Details |
A | SER82-CYS93 |