4CAB
The refined structure of catalase DR1998 from Deinococcus radiodurans at 2.6 A resolution
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 | 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 | 0003824 | molecular_function | catalytic activity |
| 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 | 0003824 | molecular_function | catalytic activity |
| 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 | 0003824 | molecular_function | catalytic activity |
| 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 537 |
| Chain | Residue |
| A | ARG78 |
| A | PHE172 |
| A | VAL228 |
| A | ASN229 |
| A | ASP310 |
| A | PHE345 |
| A | MET361 |
| A | ARG365 |
| A | SER368 |
| A | TYR369 |
| A | THR372 |
| A | VAL79 |
| A | GLN373 |
| A | ARG376 |
| A | HOH2023 |
| B | LEU67 |
| B | ASP71 |
| A | VAL80 |
| A | HIS81 |
| A | ARG123 |
| A | GLY142 |
| A | VAL157 |
| A | GLY158 |
| A | ASN159 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 1537 |
| Chain | Residue |
| A | ARG36 |
| A | HIS69 |
| A | ARG374 |
| A | PRO379 |
| A | ASN380 |
| A | LEU382 |
| A | HOH2109 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1538 |
| Chain | Residue |
| A | LYS66 |
| A | ASN396 |
| A | HOH2002 |
| A | HOH2116 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1539 |
| Chain | Residue |
| A | ARG487 |
| B | LEU422 |
| B | LEU423 |
| D | GLU509 |
| D | GLN512 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 537 |
| Chain | Residue |
| A | LEU67 |
| A | ASP71 |
| B | ARG78 |
| B | VAL79 |
| B | VAL80 |
| B | HIS81 |
| B | ARG123 |
| B | GLY142 |
| B | VAL157 |
| B | GLY158 |
| B | ASN159 |
| B | PHE172 |
| B | VAL228 |
| B | ASN229 |
| B | ASP310 |
| B | PHE345 |
| B | MET361 |
| B | ARG365 |
| B | SER368 |
| B | TYR369 |
| B | THR372 |
| B | GLN373 |
| B | ARG376 |
| B | HOH2025 |
| B | HOH2086 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 1537 |
| Chain | Residue |
| B | ARG36 |
| B | HIS69 |
| B | ARG374 |
| B | PRO379 |
| B | ASN380 |
| B | LEU382 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1538 |
| Chain | Residue |
| B | ARG254 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1002 |
| Chain | Residue |
| A | HOH2027 |
| B | LYS66 |
| B | ASN396 |
| B | HOH2002 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM C 537 |
| Chain | Residue |
| C | HOH2038 |
| C | HOH2123 |
| C | LEU67 |
| C | ASP71 |
| C | ARG78 |
| C | VAL79 |
| C | VAL80 |
| C | HIS81 |
| C | ARG123 |
| C | VAL157 |
| C | GLY158 |
| C | ASN159 |
| C | ALA169 |
| C | PHE172 |
| C | VAL228 |
| C | ASN229 |
| C | ASP310 |
| C | PHE345 |
| C | MET361 |
| C | ARG365 |
| C | SER368 |
| C | TYR369 |
| C | THR372 |
| C | GLN373 |
| C | ARG376 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 1537 |
| Chain | Residue |
| C | ARG439 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL C 1538 |
| Chain | Residue |
| C | ARG374 |
| C | PRO379 |
| C | ASN380 |
| C | TYR381 |
| C | LEU382 |
| D | ARG36 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 1002 |
| Chain | Residue |
| C | LYS66 |
| D | ASN396 |
| site_id | BC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM D 537 |
| Chain | Residue |
| D | LEU67 |
| D | ASP71 |
| D | ARG78 |
| D | VAL79 |
| D | VAL80 |
| D | HIS81 |
| D | ARG123 |
| D | VAL157 |
| D | GLY158 |
| D | ASN159 |
| D | PHE172 |
| D | VAL228 |
| D | ASN229 |
| D | PHE345 |
| D | MET361 |
| D | ARG365 |
| D | SER368 |
| D | TYR369 |
| D | THR372 |
| D | GLN373 |
| D | ARG376 |
| D | HOH2015 |
| D | HOH2030 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 1537 |
| Chain | Residue |
| C | ARG36 |
| D | ARG374 |
| D | PRO379 |
| D | ASN380 |
| D | LEU382 |
Functional Information from PROSITE/UniProt
| site_id | PS00437 |
| Number of Residues | 9 |
| Details | CATALASE_1 Catalase proximal heme-ligand signature. RTFSYsDTQ |
| Chain | Residue | Details |
| A | ARG365-GLN373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS81 | |
| A | ASN159 | |
| B | HIS81 | |
| B | ASN159 | |
| C | HIS81 | |
| C | ASN159 | |
| D | HIS81 | |
| D | ASN159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR369 | |
| B | TYR369 | |
| C | TYR369 | |
| D | TYR369 |
