Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0045454 | biological_process | cell redox homeostasis |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0045454 | biological_process | cell redox homeostasis |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019430 | biological_process | removal of superoxide radicals |
C | 0045454 | biological_process | cell redox homeostasis |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019430 | biological_process | removal of superoxide radicals |
D | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAP A4001 |
Chain | Residue |
A | ARG126 |
A | GLN192 |
A | TYR195 |
A | ILE247 |
A | GLY248 |
A | LEU293 |
A | GLY294 |
A | ARG296 |
A | HOH5067 |
A | HOH5128 |
A | HOH5176 |
A | LEU128 |
A | HOH5179 |
A | HOH5211 |
B | ARG314 |
A | GLY163 |
A | ASP164 |
A | SER165 |
A | GLU168 |
A | ARG185 |
A | ARG186 |
A | LYS190 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAP B4002 |
Chain | Residue |
A | ARG314 |
B | ARG126 |
B | LEU128 |
B | GLY163 |
B | ASP164 |
B | SER165 |
B | ARG185 |
B | ARG186 |
B | LYS190 |
B | GLN192 |
B | TYR195 |
B | ILE247 |
B | GLY248 |
B | LEU293 |
B | GLY294 |
B | HOH5001 |
B | HOH5025 |
B | HOH5036 |
B | HOH5045 |
B | HOH5050 |
B | HOH5069 |
B | HOH5085 |
B | HOH5090 |
B | HOH5184 |
B | HOH5196 |
B | HOH5198 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAP C4003 |
Chain | Residue |
C | ARG126 |
C | LEU128 |
C | ASP164 |
C | SER165 |
C | GLU168 |
C | ARG185 |
C | LYS190 |
C | GLN192 |
C | TYR195 |
C | ILE247 |
C | GLY248 |
C | LEU293 |
C | GLY294 |
C | HOH5012 |
C | HOH5113 |
C | HOH5186 |
D | ARG314 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP D4004 |
Chain | Residue |
C | ARG314 |
D | ARG126 |
D | GLY163 |
D | ASP164 |
D | SER165 |
D | ARG185 |
D | ARG186 |
D | LYS190 |
D | GLN192 |
D | TYR195 |
D | ILE247 |
D | GLY248 |
D | LEU293 |
D | GLY294 |
D | HOH5109 |
D | HOH5154 |
D | HOH5182 |
D | HOH5331 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAP A4005 |
Chain | Residue |
A | ASP287 |
A | HOH5032 |
A | HOH5046 |
A | HOH5088 |
A | HOH5223 |
A | HOH5290 |
A | HOH5296 |
A | HOH5322 |
A | GLY22 |
A | LEU23 |
A | GLY24 |
A | PRO25 |
A | ALA26 |
A | GLY45 |
A | GLU46 |
A | THR47 |
A | GLY50 |
A | GLN51 |
A | ASP90 |
A | VAL92 |
A | GLY120 |
A | ILE121 |
A | GLY122 |
A | GLY286 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP B4006 |
Chain | Residue |
B | VAL21 |
B | GLY22 |
B | LEU23 |
B | GLY24 |
B | PRO25 |
B | ALA26 |
B | GLY45 |
B | GLU46 |
B | THR47 |
B | GLY50 |
B | GLN51 |
B | ASP90 |
B | ILE91 |
B | VAL92 |
B | GLY120 |
B | ILE121 |
B | GLY122 |
B | GLY286 |
B | ASP287 |
B | HOH5059 |
B | HOH5071 |
B | HOH5108 |
B | HOH5264 |
site_id | AC7 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAP C4007 |
Chain | Residue |
C | VAL21 |
C | GLY22 |
C | LEU23 |
C | GLY24 |
C | PRO25 |
C | ALA26 |
C | GLY45 |
C | GLU46 |
C | THR47 |
C | GLY50 |
C | GLN51 |
C | ASP90 |
C | ILE91 |
C | VAL92 |
C | GLY120 |
C | ILE121 |
C | GLY122 |
C | GLY286 |
C | ASP287 |
C | HOH5003 |
C | HOH5013 |
C | HOH5018 |
C | HOH5199 |
C | HOH5249 |
C | HOH5327 |
site_id | AC8 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAP D4008 |
Chain | Residue |
D | GLY22 |
D | LEU23 |
D | GLY24 |
D | PRO25 |
D | ALA26 |
D | GLY45 |
D | GLU46 |
D | THR47 |
D | GLY50 |
D | GLN51 |
D | ASP90 |
D | ILE91 |
D | VAL92 |
D | GLY120 |
D | ILE121 |
D | GLY122 |
D | GLY286 |
D | ASP287 |
D | HOH5017 |
D | HOH5144 |
D | HOH5217 |
D | HOH5325 |
Functional Information from PROSITE/UniProt
site_id | PS00573 |
Number of Residues | 21 |
Details | PYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CsvCDApl..FknrvVaVIGGGD |
Chain | Residue | Details |
A | CYS144-ASP164 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
A | ASP148 | |
A | CYS144 | |
A | CYS147 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
B | ASP148 | |
B | CYS144 | |
B | CYS147 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
C | ASP148 | |
C | CYS144 | |
C | CYS147 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
D | ASP148 | |
D | CYS144 | |
D | CYS147 | |