3RGP
Structural and Kinetic Analysis of the Beef liver Catalase complexed with Nitric Oxide
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 | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0006979 | biological_process | response to oxidative stress |
A | 0019899 | molecular_function | enzyme binding |
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 | 0051781 | biological_process | positive regulation of cell division |
A | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
A | 0062151 | cellular_component | catalase complex |
B | 0004096 | molecular_function | catalase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0006979 | biological_process | response to oxidative stress |
B | 0019899 | molecular_function | enzyme binding |
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 | 0051781 | biological_process | positive regulation of cell division |
B | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
B | 0062151 | cellular_component | catalase complex |
C | 0004096 | molecular_function | catalase activity |
C | 0004601 | molecular_function | peroxidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005777 | cellular_component | peroxisome |
C | 0005782 | cellular_component | peroxisomal matrix |
C | 0006979 | biological_process | response to oxidative stress |
C | 0019899 | molecular_function | enzyme binding |
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 | 0051781 | biological_process | positive regulation of cell division |
C | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
C | 0062151 | cellular_component | catalase complex |
D | 0004096 | molecular_function | catalase activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005777 | cellular_component | peroxisome |
D | 0005782 | cellular_component | peroxisomal matrix |
D | 0006979 | biological_process | response to oxidative stress |
D | 0019899 | molecular_function | enzyme binding |
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 | 0051781 | biological_process | positive regulation of cell division |
D | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
D | 0062151 | cellular_component | catalase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE HEM A 1 |
Chain | Residue |
A | ARG71 |
A | PHE152 |
A | ALA157 |
A | PHE160 |
A | GLY215 |
A | SER216 |
A | PHE333 |
A | MET349 |
A | ARG353 |
A | TYR357 |
A | THR360 |
A | VAL72 |
A | HIS361 |
A | ARG364 |
A | NO502 |
A | HOH504 |
A | HOH523 |
A | HOH548 |
D | MET60 |
D | ASP64 |
A | VAL73 |
A | HIS74 |
A | ARG111 |
A | GLY130 |
A | VAL145 |
A | GLY146 |
A | ASN147 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO A 502 |
Chain | Residue |
A | HEM1 |
A | HIS74 |
A | PHE160 |
A | HOH864 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE HEM B 1 |
Chain | Residue |
B | ARG71 |
B | VAL72 |
B | VAL73 |
B | HIS74 |
B | ARG111 |
B | GLY130 |
B | VAL145 |
B | GLY146 |
B | ASN147 |
B | ALA157 |
B | PHE160 |
B | GLY215 |
B | SER216 |
B | LEU298 |
B | PHE333 |
B | MET349 |
B | ARG353 |
B | TYR357 |
B | THR360 |
B | HIS361 |
B | ARG364 |
B | NO502 |
B | HOH508 |
B | HOH533 |
B | HOH556 |
B | HOH977 |
B | HOH1360 |
C | MET60 |
C | ASP64 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO B 502 |
Chain | Residue |
B | HEM1 |
B | VAL73 |
B | HIS74 |
B | PHE160 |
B | HOH977 |
site_id | AC5 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HEM C 1 |
Chain | Residue |
B | MET60 |
B | ASP64 |
C | ARG71 |
C | VAL72 |
C | VAL73 |
C | HIS74 |
C | ARG111 |
C | GLY130 |
C | VAL145 |
C | GLY146 |
C | ASN147 |
C | ALA157 |
C | PHE160 |
C | GLY215 |
C | SER216 |
C | LEU298 |
C | PHE333 |
C | MET349 |
C | ARG353 |
C | ALA356 |
C | TYR357 |
C | THR360 |
C | HIS361 |
C | ARG364 |
C | NO502 |
C | HOH519 |
C | HOH543 |
C | HOH574 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO C 502 |
Chain | Residue |
C | HEM1 |
C | HIS74 |
C | PHE160 |
C | TYR357 |
C | HOH1185 |
site_id | AC7 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE HEM D 1 |
Chain | Residue |
A | ASP64 |
D | ARG71 |
D | VAL72 |
D | VAL73 |
D | HIS74 |
D | ARG111 |
D | GLY130 |
D | VAL145 |
D | GLY146 |
D | ASN147 |
D | ALA157 |
D | PHE160 |
D | GLY215 |
D | SER216 |
D | PHE333 |
D | MET349 |
D | ARG353 |
D | ALA356 |
D | TYR357 |
D | THR360 |
D | HIS361 |
D | ARG364 |
D | NO502 |
D | HOH504 |
D | HOH529 |
D | HOH595 |
A | MET60 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO D 502 |
Chain | Residue |
D | HEM1 |
D | HIS74 |
D | PHE160 |
D | TYR357 |
D | HOH727 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661 |
Chain | Residue | Details |
A | HIS74 | |
B | HIS74 | |
C | HIS74 | |
D | HIS74 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013 |
Chain | Residue | Details |
A | ASN147 | |
B | ASN147 | |
C | ASN147 | |
D | ASN147 |
site_id | SWS_FT_FI3 |
Number of Residues | 44 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC |
Chain | Residue | Details |
A | HIS193 | |
A | THR444 | |
A | PHE445 | |
B | HIS193 | |
B | PHE197 | |
B | SER200 | |
B | ARG202 | |
B | TYR214 | |
B | LYS236 | |
B | TRP302 | |
B | HIS304 | |
A | PHE197 | |
B | GLN441 | |
B | THR444 | |
B | PHE445 | |
C | HIS193 | |
C | PHE197 | |
C | SER200 | |
C | ARG202 | |
C | TYR214 | |
C | LYS236 | |
C | TRP302 | |
A | SER200 | |
C | HIS304 | |
C | GLN441 | |
C | THR444 | |
C | PHE445 | |
D | HIS193 | |
D | PHE197 | |
D | SER200 | |
D | ARG202 | |
D | TYR214 | |
D | LYS236 | |
A | ARG202 | |
D | TRP302 | |
D | HIS304 | |
D | GLN441 | |
D | THR444 | |
D | PHE445 | |
A | TYR214 | |
A | LYS236 | |
A | TRP302 | |
A | HIS304 | |
A | GLN441 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | ASN212 | |
B | ASN212 | |
C | ASN212 | |
D | ASN212 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC |
Chain | Residue | Details |
A | TYR357 | |
B | TYR357 | |
C | TYR357 | |
D | TYR357 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040 |
Chain | Residue | Details |
A | SER8 | |
B | SER8 | |
C | SER8 | |
D | SER8 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | LYS12 | |
A | LYS220 | |
B | LYS12 | |
B | LYS220 | |
C | LYS12 | |
C | LYS220 | |
D | LYS12 | |
D | LYS220 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | LYS232 | |
A | LYS498 | |
B | LYS232 | |
B | LYS498 | |
C | LYS232 | |
C | LYS498 | |
D | LYS232 | |
D | LYS498 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | SER416 | |
A | SER433 | |
B | SER416 | |
B | SER433 | |
C | SER416 | |
C | SER433 | |
D | SER416 | |
D | SER433 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270 |
Chain | Residue | Details |
A | LYS448 | |
A | LYS479 | |
B | LYS448 | |
B | LYS479 | |
C | LYS448 | |
C | LYS479 | |
D | LYS448 | |
D | LYS479 |