2CCD
Crystal structure of the catalase-peroxidase (KatG) and S315T mutant from Mycobacterium tuberculosis
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 | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A1741 |
| Chain | Residue |
| A | PRO100 |
| A | GLY273 |
| A | LYS274 |
| A | THR275 |
| A | HIS276 |
| A | THR314 |
| A | THR315 |
| A | TRP321 |
| A | THR380 |
| A | PHE408 |
| A | TRP412 |
| A | ILE103 |
| A | HOH2035 |
| A | HOH2339 |
| A | HOH2340 |
| A | TRP107 |
| A | VAL230 |
| A | PRO232 |
| A | LEU265 |
| A | ILE266 |
| A | GLY269 |
| A | HIS270 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B1741 |
| Chain | Residue |
| B | PRO100 |
| B | LEU101 |
| B | ILE103 |
| B | TRP107 |
| B | VAL230 |
| B | PRO232 |
| B | PHE252 |
| B | LEU265 |
| B | GLY269 |
| B | HIS270 |
| B | GLY273 |
| B | LYS274 |
| B | THR275 |
| B | HIS276 |
| B | THR314 |
| B | THR315 |
| B | TRP321 |
| B | LEU378 |
| B | THR380 |
| B | PHE408 |
| B | HOH2253 |
| B | HOH2254 |
| B | HOH2255 |
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 |
