Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004096 | molecular_function | catalase activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0006979 | biological_process | response to oxidative stress |
A | 0019899 | molecular_function | enzyme binding |
A | 0020037 | molecular_function | heme binding |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051781 | biological_process | positive regulation of cell division |
A | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
A | 0062151 | cellular_component | catalase complex |
B | 0004096 | molecular_function | catalase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0006979 | biological_process | response to oxidative stress |
B | 0019899 | molecular_function | enzyme binding |
B | 0020037 | molecular_function | heme binding |
B | 0042542 | biological_process | response to hydrogen peroxide |
B | 0042744 | biological_process | hydrogen peroxide catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051781 | biological_process | positive regulation of cell division |
B | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
B | 0062151 | cellular_component | catalase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 507 |
Chain | Residue |
A | ARG71 |
A | ALA157 |
A | PHE160 |
A | LEU298 |
A | PHE333 |
A | MET349 |
A | ARG353 |
A | ALA356 |
A | TYR357 |
A | THR360 |
A | HIS361 |
A | VAL72 |
A | ARG364 |
A | HOH509 |
A | HOH511 |
B | ASP64 |
A | VAL73 |
A | HIS74 |
A | ARG111 |
A | GLY130 |
A | VAL145 |
A | GLY146 |
A | ASN147 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NDP A 508 |
Chain | Residue |
A | HIS193 |
A | PHE197 |
A | SER200 |
A | ARG202 |
A | HIS234 |
A | LYS236 |
A | ILE241 |
A | VAL301 |
A | TRP302 |
A | PRO303 |
A | HIS304 |
A | GLN441 |
A | THR444 |
A | PHE445 |
A | VAL449 |
A | HOH512 |
A | HOH513 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 507 |
Chain | Residue |
A | ASP64 |
B | ARG71 |
B | VAL72 |
B | VAL73 |
B | HIS74 |
B | ARG111 |
B | GLY130 |
B | VAL145 |
B | GLY146 |
B | ASN147 |
B | ALA157 |
B | PHE160 |
B | LEU298 |
B | PHE333 |
B | MET349 |
B | ARG353 |
B | ALA356 |
B | TYR357 |
B | THR360 |
B | HIS361 |
B | ARG364 |
B | HOH517 |
B | HOH519 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NDP B 508 |
Chain | Residue |
B | HIS193 |
B | PHE197 |
B | SER200 |
B | ARG202 |
B | HIS234 |
B | LYS236 |
B | ILE241 |
B | VAL301 |
B | TRP302 |
B | PRO303 |
B | HIS304 |
B | GLN441 |
B | THR444 |
B | PHE445 |
B | VAL449 |
B | HOH520 |
B | HOH521 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661 |
Chain | Residue | Details |
A | ALA75 | |
B | ALA75 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 |
Chain | Residue | Details |
A | ASN148 | |
B | ASN148 |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC |
Chain | Residue | Details |
A | GLN194 | |
A | PHE445 | |
A | TYR446 | |
B | GLN194 | |
B | LEU198 | |
B | ASP201 | |
B | GLY203 | |
B | GLY215 | |
B | THR237 | |
B | PRO303 | |
B | GLY305 | |
A | LEU198 | |
B | VAL442 | |
B | PHE445 | |
B | TYR446 | |
A | ASP201 | |
A | GLY203 | |
A | GLY215 | |
A | THR237 | |
A | PRO303 | |
A | GLY305 | |
A | VAL442 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | GLY213 | |
B | GLY213 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC |
Chain | Residue | Details |
A | PRO358 | |
B | PRO358 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine; alternate => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | ASP2 | |
B | ASP2 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | ASP9 | |
B | ASP9 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | HIS13 | |
A | LEU221 | |
B | HIS13 | |
B | LEU221 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | PHE233 | |
A | TYR499 | |
B | PHE233 | |
B | TYR499 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | ALA417 | |
A | ALA434 | |
B | ALA417 | |
B | ALA434 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | VAL449 | |
A | ASN480 | |
B | VAL449 | |
B | ASN480 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
A | SER113 | |
A | HIS74 | |
A | ASN147 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
B | SER113 | |
B | HIS74 | |
B | ASN147 |