4E37
Crystal Structure of P. aeruginosa catalase, KatA tetramer
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 | 0006979 | biological_process | response to oxidative stress |
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 | 0098869 | biological_process | cellular oxidant detoxification |
B | 0004096 | molecular_function | catalase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006979 | biological_process | response to oxidative stress |
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 | 0098869 | biological_process | cellular oxidant detoxification |
C | 0004096 | molecular_function | catalase activity |
C | 0004601 | molecular_function | peroxidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006979 | biological_process | response to oxidative stress |
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 | 0098869 | biological_process | cellular oxidant detoxification |
D | 0004096 | molecular_function | catalase activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006979 | biological_process | response to oxidative stress |
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 | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 500 |
Chain | Residue |
A | ARG52 |
A | PHE141 |
A | SER197 |
A | HIS198 |
A | PHE314 |
A | MET330 |
A | ARG334 |
A | SER337 |
A | TYR338 |
A | HIS342 |
A | ARG345 |
A | HIS55 |
A | HOH619 |
A | HOH621 |
A | HOH628 |
A | HOH697 |
B | ASP45 |
A | ARG92 |
A | GLY111 |
A | PHE112 |
A | VAL126 |
A | GLY127 |
A | ASN128 |
A | PRO138 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NDP A 501 |
Chain | Residue |
A | PRO131 |
A | HIS174 |
A | SER181 |
A | ARG183 |
A | HIS193 |
A | HIS215 |
A | VAL282 |
A | TRP283 |
A | PRO284 |
A | HIS285 |
A | GLN423 |
A | LEU427 |
A | LEU430 |
A | PHE431 |
A | HOH709 |
A | HOH717 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 500 |
Chain | Residue |
A | ASP45 |
B | ARG52 |
B | HIS55 |
B | ARG92 |
B | GLY111 |
B | PHE112 |
B | VAL126 |
B | GLY127 |
B | ASN128 |
B | PRO138 |
B | PHE141 |
B | SER197 |
B | HIS198 |
B | PHE314 |
B | MET330 |
B | ARG334 |
B | SER337 |
B | TYR338 |
B | HIS342 |
B | ARG345 |
B | HOH621 |
B | HOH641 |
B | HOH679 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NDP B 501 |
Chain | Residue |
B | PRO131 |
B | HIS174 |
B | SER181 |
B | ARG183 |
B | HIS193 |
B | HIS215 |
B | VAL282 |
B | TRP283 |
B | PRO284 |
B | HIS285 |
B | GLN423 |
B | ALA426 |
B | LEU427 |
B | LEU430 |
B | PHE431 |
B | HOH705 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM C 500 |
Chain | Residue |
C | HOH607 |
C | HOH628 |
C | HOH670 |
D | ASP45 |
C | ARG52 |
C | HIS55 |
C | ARG92 |
C | GLY111 |
C | PHE112 |
C | VAL126 |
C | GLY127 |
C | ASN128 |
C | PRO138 |
C | PHE141 |
C | SER197 |
C | HIS198 |
C | PHE314 |
C | MET330 |
C | ARG334 |
C | SER337 |
C | TYR338 |
C | HIS342 |
C | ARG345 |
C | HOH604 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NDP C 501 |
Chain | Residue |
C | PRO131 |
C | HIS174 |
C | SER181 |
C | ARG183 |
C | HIS193 |
C | HIS215 |
C | VAL282 |
C | TRP283 |
C | PRO284 |
C | HIS285 |
C | GLN423 |
C | LEU427 |
C | LEU430 |
C | PHE431 |
C | HOH699 |
site_id | AC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM D 500 |
Chain | Residue |
D | ARG52 |
D | OMT54 |
D | HIS55 |
D | ARG92 |
D | VAL126 |
D | GLY127 |
D | ASN128 |
D | PRO138 |
D | PHE141 |
D | GLY196 |
D | SER197 |
D | HIS198 |
D | PHE314 |
D | MET330 |
D | ARG334 |
D | SER337 |
D | TYR338 |
D | HIS342 |
D | ARG345 |
D | HOH615 |
D | HOH627 |
D | HOH638 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NDP D 501 |
Chain | Residue |
D | PRO131 |
D | HIS174 |
D | SER181 |
D | ARG183 |
D | HIS193 |
D | HIS215 |
D | VAL282 |
D | TRP283 |
D | PRO284 |
D | HIS285 |
D | GLN423 |
D | LEU427 |
D | PHE431 |
D | HOH613 |
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 | HIS55 | |
A | ASN128 | |
B | HIS55 | |
B | ASN128 | |
C | HIS55 | |
C | ASN128 | |
D | HIS55 | |
D | ASN128 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000250 |
Chain | Residue | Details |
A | TYR338 | |
B | TYR338 | |
C | TYR338 | |
D | TYR338 |