1M7S
Crystal Structure Analysis of Catalase CatF of Pseudomonas syringae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004096 | molecular_function | catalase activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005777 | cellular_component | peroxisome |
A | 0005886 | cellular_component | plasma membrane |
A | 0006979 | biological_process | response to oxidative stress |
A | 0020037 | molecular_function | heme binding |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0042597 | cellular_component | periplasmic space |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0003824 | molecular_function | catalytic activity |
B | 0004096 | molecular_function | catalase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005777 | cellular_component | peroxisome |
B | 0005886 | cellular_component | plasma membrane |
B | 0006979 | biological_process | response to oxidative stress |
B | 0020037 | molecular_function | heme binding |
B | 0042542 | biological_process | response to hydrogen peroxide |
B | 0042597 | cellular_component | periplasmic space |
B | 0042744 | biological_process | hydrogen peroxide catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
C | 0003824 | molecular_function | catalytic activity |
C | 0004096 | molecular_function | catalase activity |
C | 0004601 | molecular_function | peroxidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005777 | cellular_component | peroxisome |
C | 0005886 | cellular_component | plasma membrane |
C | 0006979 | biological_process | response to oxidative stress |
C | 0020037 | molecular_function | heme binding |
C | 0042542 | biological_process | response to hydrogen peroxide |
C | 0042597 | cellular_component | periplasmic space |
C | 0042744 | biological_process | hydrogen peroxide catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0098869 | biological_process | cellular oxidant detoxification |
D | 0003824 | molecular_function | catalytic activity |
D | 0004096 | molecular_function | catalase activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005777 | cellular_component | peroxisome |
D | 0005886 | cellular_component | plasma membrane |
D | 0006979 | biological_process | response to oxidative stress |
D | 0020037 | molecular_function | heme binding |
D | 0042542 | biological_process | response to hydrogen peroxide |
D | 0042597 | cellular_component | periplasmic space |
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 | 27 |
Details | BINDING SITE FOR RESIDUE HEM A 600 |
Chain | Residue |
A | ARG75 |
A | PHE163 |
A | VAL219 |
A | HIS220 |
A | MET334 |
A | LEU350 |
A | GLY353 |
A | ARG354 |
A | SER357 |
A | TYR358 |
A | THR361 |
A | VAL77 |
A | GLN362 |
A | ARG365 |
A | HOH1019 |
A | HOH1202 |
A | HOH1270 |
A | HOH1673 |
A | HOH3059 |
D | ASP68 |
A | HIS78 |
A | ARG114 |
A | GLY133 |
A | VAL148 |
A | GLY149 |
A | ASN150 |
A | PHE155 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM B 600 |
Chain | Residue |
B | ARG75 |
B | VAL76 |
B | VAL77 |
B | HIS78 |
B | ARG114 |
B | GLY133 |
B | VAL148 |
B | GLY149 |
B | ASN150 |
B | PHE163 |
B | VAL219 |
B | HIS220 |
B | LEU350 |
B | GLY353 |
B | ARG354 |
B | SER357 |
B | TYR358 |
B | THR361 |
B | GLN362 |
B | ARG365 |
B | HOH1066 |
B | HOH1266 |
B | HOH1300 |
B | HOH3125 |
C | ASP68 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEM C 600 |
Chain | Residue |
B | ASP68 |
C | ARG75 |
C | VAL76 |
C | VAL77 |
C | HIS78 |
C | ARG114 |
C | GLY133 |
C | VAL148 |
C | GLY149 |
C | ASN150 |
C | PHE155 |
C | PHE163 |
C | VAL219 |
C | HIS220 |
C | LEU350 |
C | GLY353 |
C | ARG354 |
C | SER357 |
C | TYR358 |
C | THR361 |
C | GLN362 |
C | ARG365 |
C | HOH1061 |
C | HOH1194 |
C | HOH1335 |
C | HOH1358 |
site_id | AC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM D 600 |
Chain | Residue |
D | HOH1004 |
D | HOH1012 |
D | HOH1148 |
D | HOH1242 |
D | ARG75 |
D | VAL76 |
D | VAL77 |
D | HIS78 |
D | ARG114 |
D | GLY133 |
D | VAL148 |
D | GLY149 |
D | ASN150 |
D | PHE155 |
D | PHE163 |
D | VAL219 |
D | HIS220 |
D | LEU350 |
D | GLY353 |
D | ARG354 |
D | SER357 |
D | TYR358 |
D | THR361 |
D | GLN362 |
D | ARG365 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 |
Chain | Residue | Details |
A | HIS78 | |
A | ASN150 | |
B | HIS78 | |
B | ASN150 | |
C | HIS78 | |
C | ASN150 | |
D | HIS78 | |
D | ASN150 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000250 |
Chain | Residue | Details |
A | TYR358 | |
B | TYR358 | |
C | TYR358 | |
D | TYR358 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
A | SER116 | |
A | ASN150 | |
A | HIS78 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
B | SER116 | |
B | ASN150 | |
B | HIS78 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
C | SER116 | |
C | ASN150 | |
C | HIS78 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
D | SER116 | |
D | ASN150 | |
D | HIS78 |