4AJ9
Catalase 3 from Neurospora crassa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004096 | molecular_function | catalase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004096 | molecular_function | catalase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004096 | molecular_function | catalase activity |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042744 | biological_process | hydrogen peroxide catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004096 | molecular_function | catalase activity |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0042744 | biological_process | hydrogen peroxide catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 1716 |
| Chain | Residue |
| A | VAL143 |
| A | ASP155 |
| A | VAL156 |
| A | PHE181 |
| A | VAL195 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1718 |
| Chain | Residue |
| B | VAL195 |
| B | VAL143 |
| B | ASP155 |
| B | VAL156 |
| B | PHE181 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 1721 |
| Chain | Residue |
| C | VAL143 |
| C | ALA144 |
| C | ASP155 |
| C | VAL156 |
| C | PHE181 |
| C | VAL195 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT D 1717 |
| Chain | Residue |
| D | VAL143 |
| D | ASP155 |
| D | VAL156 |
| D | PHE181 |
| D | VAL195 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 1717 |
| Chain | Residue |
| A | ASN176 |
| A | ASN234 |
| A | PRO237 |
| A | HIS242 |
| A | MET243 |
| A | ALA274 |
| A | ILE558 |
| A | HOH2196 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1719 |
| Chain | Residue |
| B | ASN176 |
| B | PRO237 |
| B | HIS242 |
| B | LYS273 |
| B | ALA274 |
| B | HOH2144 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT C 1722 |
| Chain | Residue |
| C | ASN176 |
| C | PRO237 |
| C | HIS242 |
| C | MET243 |
| C | LYS273 |
| C | ALA274 |
| C | ILE558 |
| C | HOH2128 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT D 1718 |
| Chain | Residue |
| D | ASN176 |
| D | ASN234 |
| D | PRO237 |
| D | HIS242 |
| D | MET243 |
| D | LYS273 |
| D | ALA274 |
| D | HOH2112 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1719 |
| Chain | Residue |
| D | ARG409 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1723 |
| Chain | Residue |
| C | VAL552 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1720 |
| Chain | Residue |
| B | ARG409 |
| B | VAL414 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1718 |
| Chain | Residue |
| A | LYS441 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1719 |
| Chain | Residue |
| A | GLU317 |
| A | GLY460 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1720 |
| Chain | Residue |
| A | GLU709 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1720 |
| Chain | Residue |
| D | TYR658 |
| D | ARG659 |
| D | ILE677 |
| D | HOH2425 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1721 |
| Chain | Residue |
| A | VAL552 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1721 |
| Chain | Residue |
| D | LYS441 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1724 |
| Chain | Residue |
| C | GLU317 |
| C | GLY460 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1721 |
| Chain | Residue |
| B | ASP200 |
| D | ILE431 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1725 |
| Chain | Residue |
| D | GLN542 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1726 |
| Chain | Residue |
| C | TYR438 |
| C | LYS441 |
| D | ASN551 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1722 |
| Chain | Residue |
| A | GLN652 |
| A | THR655 |
| A | ARG659 |
| A | 1PE1723 |
| A | HOH2630 |
| B | GLN652 |
| B | THR655 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1722 |
| Chain | Residue |
| B | TYR547 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1723 |
| Chain | Residue |
| A | PRO340 |
| B | GLY324 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1724 |
| Chain | Residue |
| B | THR600 |
| B | GLN612 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1723 |
| Chain | Residue |
| A | PHE635 |
| A | ALA640 |
| A | SER651 |
| A | 1PE1722 |
| B | ARG659 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1722 |
| Chain | Residue |
| D | ALA473 |
| D | THR474 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1724 |
| Chain | Residue |
| A | GLN612 |
| A | ALA621 |
| A | HOH2146 |
| A | HOH2577 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1723 |
| Chain | Residue |
| D | ASN551 |
| D | VAL552 |
| C | LYS441 |
| D | GLU337 |
| D | PHE338 |
| site_id | DC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1727 |
| Chain | Residue |
| C | HOH2445 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1725 |
| Chain | Residue |
| A | ASP117 |
| B | ASN487 |
| B | SER488 |
| B | HOH2465 |
| site_id | DC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE B 1726 |
| Chain | Residue |
| A | TYR115 |
| B | TRP118 |
| B | LEU341 |
| B | GLN342 |
| B | VAL343 |
| B | LEU344 |
| B | HOH2285 |
| B | HOH2553 |
| site_id | DC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 1715 |
| Chain | Residue |
| A | ARG99 |
| A | VAL100 |
| A | VAL101 |
| A | HIS102 |
| A | ARG139 |
| A | GLY158 |
| A | VAL173 |
| A | GLY174 |
| A | ASN175 |
| A | PHE180 |
| A | PHE188 |
| A | ILE248 |
| A | HIS249 |
| A | PHE365 |
| A | LEU381 |
| A | ARG385 |
| A | SER388 |
| A | TYR389 |
| A | GLN393 |
| A | ARG396 |
| A | HOH2101 |
| A | HOH2105 |
| A | HOH2147 |
| A | HOH2362 |
| site_id | DC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 1717 |
| Chain | Residue |
| B | ARG99 |
| B | VAL100 |
| B | VAL101 |
| B | HIS102 |
| B | ARG139 |
| B | GLY158 |
| B | VAL173 |
| B | GLY174 |
| B | ASN175 |
| B | PHE180 |
| B | PHE188 |
| B | ILE248 |
| B | HIS249 |
| B | PHE365 |
| B | LEU381 |
| B | ARG385 |
| B | SER388 |
| B | TYR389 |
| B | THR392 |
| B | GLN393 |
| B | ARG396 |
| B | HOH2071 |
| B | HOH2073 |
| B | HOH2108 |
| B | HOH2300 |
| site_id | DC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 1720 |
| Chain | Residue |
| C | ARG99 |
| C | VAL100 |
| C | VAL101 |
| C | HIS102 |
| C | ARG139 |
| C | GLY158 |
| C | VAL173 |
| C | GLY174 |
| C | ASN175 |
| C | PHE180 |
| C | PHE188 |
| C | ILE248 |
| C | HIS249 |
| C | PHE365 |
| C | LEU381 |
| C | ARG385 |
| C | SER388 |
| C | TYR389 |
| C | THR392 |
| C | GLN393 |
| C | ARG396 |
| C | HOH2051 |
| C | HOH2088 |
| C | HOH2285 |
| site_id | DC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM D 1716 |
| Chain | Residue |
| C | LEU88 |
| D | ARG99 |
| D | VAL100 |
| D | VAL101 |
| D | HIS102 |
| D | ARG139 |
| D | GLY158 |
| D | VAL173 |
| D | GLY174 |
| D | ASN175 |
| D | PHE188 |
| D | ILE248 |
| D | HIS249 |
| D | PHE365 |
| D | LEU381 |
| D | ARG385 |
| D | SER388 |
| D | TYR389 |
| D | THR392 |
| D | GLN393 |
| D | ARG396 |
| D | HOH2042 |
| D | HOH2044 |
| D | HOH2078 |
| D | HOH2255 |
Functional Information from PROSITE/UniProt
| site_id | PS00438 |
| Number of Residues | 17 |
| Details | CATALASE_2 Catalase proximal active site signature. FdHeripERvvHarGAG |
| Chain | Residue | Details |
| A | PHE91-GLY107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






