1QF7
STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004096 | molecular_function | catalase activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006972 | biological_process | hyperosmotic response |
A | 0006974 | biological_process | DNA damage response |
A | 0006979 | biological_process | response to oxidative stress |
A | 0020037 | molecular_function | heme binding |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0042802 | molecular_function | identical protein binding |
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 | 0005506 | molecular_function | iron ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006972 | biological_process | hyperosmotic response |
B | 0006974 | biological_process | DNA damage response |
B | 0006979 | biological_process | response to oxidative stress |
B | 0020037 | molecular_function | heme binding |
B | 0042744 | biological_process | hydrogen peroxide catabolic process |
B | 0042802 | molecular_function | identical protein binding |
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 | 0005506 | molecular_function | iron ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006972 | biological_process | hyperosmotic response |
C | 0006974 | biological_process | DNA damage response |
C | 0006979 | biological_process | response to oxidative stress |
C | 0020037 | molecular_function | heme binding |
C | 0042744 | biological_process | hydrogen peroxide catabolic process |
C | 0042802 | molecular_function | identical protein binding |
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 | 0005506 | molecular_function | iron ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006972 | biological_process | hyperosmotic response |
D | 0006974 | biological_process | DNA damage response |
D | 0006979 | biological_process | response to oxidative stress |
D | 0020037 | molecular_function | heme binding |
D | 0042744 | biological_process | hydrogen peroxide catabolic process |
D | 0042802 | molecular_function | identical protein binding |
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 | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 754 |
Chain | Residue |
A | ARG125 |
A | ILE126 |
A | VAL127 |
A | HIS128 |
A | ARG165 |
A | GLY184 |
A | VAL199 |
A | GLY200 |
A | ASN201 |
A | PHE214 |
A | ILE274 |
A | HIS275 |
A | PHE391 |
A | LEU407 |
A | ARG411 |
A | SER414 |
A | TYR415 |
A | THR418 |
A | GLN419 |
A | ARG422 |
A | HOH775 |
A | HOH824 |
A | HOH856 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HEM B 754 |
Chain | Residue |
B | ARG125 |
B | ILE126 |
B | VAL127 |
B | HIS128 |
B | ARG165 |
B | GLY184 |
B | VAL199 |
B | GLY200 |
B | ASN201 |
B | PHE206 |
B | PHE214 |
B | ILE274 |
B | HIS275 |
B | PHE391 |
B | LEU407 |
B | ARG411 |
B | SER414 |
B | TYR415 |
B | THR418 |
B | GLN419 |
B | ARG422 |
B | HOH782 |
B | HOH831 |
B | HOH864 |
B | HOH1377 |
C | ASP118 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM C 754 |
Chain | Residue |
C | ARG125 |
C | ILE126 |
C | VAL127 |
C | HIS128 |
C | ARG165 |
C | GLY184 |
C | VAL199 |
C | GLY200 |
C | ASN201 |
C | PHE214 |
C | HIS275 |
C | PHE391 |
C | LEU407 |
C | ARG411 |
C | SER414 |
C | TYR415 |
C | THR418 |
C | GLN419 |
C | ARG422 |
C | HOH816 |
C | HOH864 |
C | HOH899 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM D 754 |
Chain | Residue |
D | SER414 |
D | TYR415 |
D | THR418 |
D | GLN419 |
D | ARG422 |
D | HOH829 |
D | HOH878 |
D | HOH910 |
A | ASP118 |
D | ARG125 |
D | ILE126 |
D | VAL127 |
D | HIS128 |
D | ARG165 |
D | GLY184 |
D | VAL199 |
D | GLY200 |
D | ASN201 |
D | PHE214 |
D | ILE274 |
D | HIS275 |
D | PHE391 |
D | LEU407 |
D | ARG411 |
site_id | CAA |
Number of Residues | 3 |
Details | ESSENTIAL CATALYTIC RESIDUES. |
Chain | Residue |
A | HIS128 |
A | ASN201 |
A | TYR415 |
site_id | CAB |
Number of Residues | 3 |
Details | ESSENTIAL CATALYTIC RESIDUES. |
Chain | Residue |
B | HIS128 |
B | ASN201 |
B | TYR415 |
site_id | CAC |
Number of Residues | 3 |
Details | ESSENTIAL CATALYTIC RESIDUES. |
Chain | Residue |
C | HIS128 |
C | ASN201 |
C | TYR415 |
site_id | CAD |
Number of Residues | 3 |
Details | ESSENTIAL CATALYTIC RESIDUES. |
Chain | Residue |
D | HIS128 |
D | ASN201 |
D | TYR415 |
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 | HIS128 | |
A | ASN201 | |
B | HIS128 | |
B | ASN201 | |
C | HIS128 | |
C | ASN201 | |
D | HIS128 | |
D | ASN201 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TYR415 | |
B | TYR415 | |
C | TYR415 | |
D | TYR415 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | CROSSLNK: 3'-histidyl-3-tyrosine (His-Tyr) |
Chain | Residue | Details |
A | GLN392 | |
A | TYR415 | |
B | GLN392 | |
B | TYR415 | |
C | GLN392 | |
C | TYR415 | |
D | GLN392 | |
D | TYR415 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
A | ASN201 | |
A | SER167 | |
A | HIS128 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
B | ASN201 | |
B | SER167 | |
B | HIS128 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
C | ASN201 | |
C | SER167 | |
C | HIS128 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1iph |
Chain | Residue | Details |
D | ASN201 | |
D | SER167 | |
D | HIS128 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 573 |
Chain | Residue | Details |
A | HIS128 | proton shuttle (general acid/base) |
A | ASN201 | electrostatic stabiliser |
A | GLN392 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 573 |
Chain | Residue | Details |
B | HIS128 | proton shuttle (general acid/base) |
B | ASN201 | electrostatic stabiliser |
B | GLN392 | proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 573 |
Chain | Residue | Details |
C | HIS128 | proton shuttle (general acid/base) |
C | ASN201 | electrostatic stabiliser |
C | GLN392 | proton shuttle (general acid/base) |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 573 |
Chain | Residue | Details |
D | HIS128 | proton shuttle (general acid/base) |
D | ASN201 | electrostatic stabiliser |
D | GLN392 | proton shuttle (general acid/base) |