1TH2
crystal structure of NADPH depleted bovine liver catalase complexed with azide
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 |
C | 0004096 | molecular_function | catalase activity |
C | 0004601 | molecular_function | peroxidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005777 | cellular_component | peroxisome |
C | 0005782 | cellular_component | peroxisomal matrix |
C | 0006979 | biological_process | response to oxidative stress |
C | 0019899 | molecular_function | enzyme binding |
C | 0020037 | molecular_function | heme binding |
C | 0042542 | biological_process | response to hydrogen peroxide |
C | 0042744 | biological_process | hydrogen peroxide catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051781 | biological_process | positive regulation of cell division |
C | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
C | 0062151 | cellular_component | catalase complex |
D | 0004096 | molecular_function | catalase activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005777 | cellular_component | peroxisome |
D | 0005782 | cellular_component | peroxisomal matrix |
D | 0006979 | biological_process | response to oxidative stress |
D | 0019899 | molecular_function | enzyme binding |
D | 0020037 | molecular_function | heme binding |
D | 0042542 | biological_process | response to hydrogen peroxide |
D | 0042744 | biological_process | hydrogen peroxide catabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0051781 | biological_process | positive regulation of cell division |
D | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
D | 0062151 | cellular_component | catalase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE AZI D 3000 |
Chain | Residue |
D | VAL73 |
D | HIS74 |
D | ASN147 |
D | PHE160 |
D | HEM2003 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM A 2000 |
Chain | Residue |
A | GLY130 |
A | VAL145 |
A | GLY146 |
A | ASN147 |
A | PHE333 |
A | MET349 |
A | ARG353 |
A | TYR357 |
A | THR360 |
A | HIS361 |
A | ARG364 |
A | HOH2005 |
A | HOH2012 |
A | ARG71 |
A | VAL73 |
A | HIS74 |
A | ARG111 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM B 2001 |
Chain | Residue |
B | ARG71 |
B | HIS74 |
B | ARG111 |
B | VAL145 |
B | ASN147 |
B | PHE152 |
B | PHE160 |
B | SER216 |
B | PHE333 |
B | MET349 |
B | ARG353 |
B | TYR357 |
B | THR360 |
B | HIS361 |
B | ARG364 |
B | HOH2183 |
C | MET60 |
C | PHE63 |
C | ASP64 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM C 2002 |
Chain | Residue |
B | MET60 |
C | ARG71 |
C | VAL72 |
C | VAL73 |
C | HIS74 |
C | ARG111 |
C | GLY130 |
C | GLY146 |
C | ASN147 |
C | PHE152 |
C | PHE160 |
C | SER216 |
C | PHE333 |
C | MET349 |
C | ARG353 |
C | TYR357 |
C | THR360 |
C | HIS361 |
C | ARG364 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM D 2003 |
Chain | Residue |
A | MET60 |
A | ASP64 |
D | ARG71 |
D | VAL72 |
D | VAL73 |
D | HIS74 |
D | ARG111 |
D | VAL145 |
D | GLY146 |
D | ASN147 |
D | PHE160 |
D | MET349 |
D | ARG353 |
D | TYR357 |
D | THR360 |
D | HIS361 |
D | ARG364 |
D | AZI3000 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661 |
Chain | Residue | Details |
A | ALA75 | |
B | ALA75 | |
C | ALA75 | |
D | ALA75 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 |
Chain | Residue | Details |
A | ASN148 | |
B | ASN148 | |
C | ASN148 | |
D | ASN148 |
site_id | SWS_FT_FI3 |
Number of Residues | 44 |
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 | |
C | GLN194 | |
C | LEU198 | |
C | ASP201 | |
C | GLY203 | |
C | GLY215 | |
C | THR237 | |
C | PRO303 | |
A | ASP201 | |
C | GLY305 | |
C | VAL442 | |
C | PHE445 | |
C | TYR446 | |
D | GLN194 | |
D | LEU198 | |
D | ASP201 | |
D | GLY203 | |
D | GLY215 | |
D | THR237 | |
A | GLY203 | |
D | PRO303 | |
D | GLY305 | |
D | VAL442 | |
D | PHE445 | |
D | TYR446 | |
A | GLY215 | |
A | THR237 | |
A | PRO303 | |
A | GLY305 | |
A | VAL442 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | GLY213 | |
B | GLY213 | |
C | GLY213 | |
D | GLY213 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC |
Chain | Residue | Details |
A | PRO358 | |
B | PRO358 | |
C | PRO358 | |
D | PRO358 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine; alternate => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | ASP2 | |
B | ASP2 | |
C | ASP2 | |
D | ASP2 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | ASP9 | |
B | ASP9 | |
C | ASP9 | |
D | ASP9 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | HIS13 | |
A | LEU221 | |
B | HIS13 | |
B | LEU221 | |
C | HIS13 | |
C | LEU221 | |
D | HIS13 | |
D | LEU221 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | PHE233 | |
A | TYR499 | |
B | PHE233 | |
B | TYR499 | |
C | PHE233 | |
C | TYR499 | |
D | PHE233 | |
D | TYR499 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | ALA417 | |
A | ALA434 | |
B | ALA417 | |
B | ALA434 | |
C | ALA417 | |
C | ALA434 | |
D | ALA417 | |
D | ALA434 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | VAL449 | |
A | ASN480 | |
B | VAL449 | |
B | ASN480 | |
C | VAL449 | |
C | ASN480 | |
D | VAL449 | |
D | 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 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
C | SER113 | |
C | HIS74 | |
C | ASN147 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
D | SER113 | |
D | HIS74 | |
D | ASN147 |