1SJ2
Crystal structure of Mycobacterium tuberculosis catalase-peroxidase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004096 | molecular_function | catalase activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006979 | biological_process | response to oxidative stress |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016677 | molecular_function | oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor |
A | 0020037 | molecular_function | heme binding |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0045739 | biological_process | positive regulation of DNA repair |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
A | 0070301 | biological_process | cellular response to hydrogen peroxide |
A | 0070402 | molecular_function | NADPH binding |
A | 0070404 | molecular_function | NADH binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0004096 | molecular_function | catalase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006979 | biological_process | response to oxidative stress |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016677 | molecular_function | oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor |
B | 0020037 | molecular_function | heme binding |
B | 0042744 | biological_process | hydrogen peroxide catabolic process |
B | 0045739 | biological_process | positive regulation of DNA repair |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
B | 0070301 | biological_process | cellular response to hydrogen peroxide |
B | 0070402 | molecular_function | NADPH binding |
B | 0070404 | molecular_function | NADH binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM A 1500 |
Chain | Residue |
A | PRO100 |
A | THR275 |
A | HIS276 |
A | THR314 |
A | SER315 |
A | TRP321 |
A | TRP412 |
A | HOH1504 |
A | HOH1507 |
A | HOH1769 |
A | ILE103 |
A | ARG104 |
A | TRP107 |
A | LEU265 |
A | GLY269 |
A | HIS270 |
A | GLY273 |
A | LYS274 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM B 1500 |
Chain | Residue |
B | PRO100 |
B | LEU101 |
B | ILE103 |
B | ARG104 |
B | TRP107 |
B | PRO232 |
B | LEU265 |
B | ILE266 |
B | GLY269 |
B | HIS270 |
B | GLY273 |
B | LYS274 |
B | THR275 |
B | HIS276 |
B | THR314 |
B | SER315 |
B | TRP321 |
B | THR380 |
B | TRP412 |
B | HOH2199 |
B | HOH2216 |
B | HOH2415 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 1194 |
Chain | Residue |
A | PHE62 |
A | TYR64 |
A | LYS152 |
A | GLY156 |
A | LYS157 |
A | ASP189 |
A | TRP191 |
A | HOH1527 |
A | HOH1537 |
A | HOH1551 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1195 |
Chain | Residue |
A | ARG42 |
A | LEU43 |
A | GLU607 |
A | TYR608 |
A | ASN701 |
A | HOH1545 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1196 |
Chain | Residue |
A | SER482 |
A | LEU587 |
A | LYS613 |
A | LEU616 |
A | HOH1808 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 2194 |
Chain | Residue |
B | MET58 |
B | LYS152 |
B | LYS157 |
B | ASP189 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 2195 |
Chain | Residue |
B | ARG42 |
B | LEU43 |
B | GLU607 |
B | TYR608 |
B | VAL697 |
B | ASN701 |
B | HOH2504 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 2196 |
Chain | Residue |
B | ARG484 |
B | PRO589 |
B | ALA591 |
B | LYS613 |
B | LEU616 |
B | HOH2466 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961 |
Chain | Residue | Details |
A | HIS108 | |
B | HIS108 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:18052167 |
Chain | Residue | Details |
A | TRP321 | |
B | TRP321 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:15231843, ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:24185282, ECO:0007744|PDB:1SJ2, ECO:0007744|PDB:2CCA, ECO:0007744|PDB:2CCD, ECO:0007744|PDB:4C51 |
Chain | Residue | Details |
A | HIS270 | |
B | HIS270 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961 |
Chain | Residue | Details |
A | ARG104 | |
B | ARG104 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843 |
Chain | Residue | Details |
A | TRP107 | |
B | TRP107 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843 |
Chain | Residue | Details |
A | TYR229 | |
A | MET255 | |
B | TYR229 | |
B | MET255 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ARG104 | |
A | ASP137 | |
A | HIS108 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
B | ARG104 | |
B | ASP137 | |
B | HIS108 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ASN138 | |
A | ARG104 | |
A | HIS108 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
B | ASN138 | |
B | ARG104 | |
B | HIS108 |