3QWB
Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1 complexed with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0035925 | molecular_function | mRNA 3'-UTR AU-rich region binding |
| B | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0035925 | molecular_function | mRNA 3'-UTR AU-rich region binding |
| C | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0035925 | molecular_function | mRNA 3'-UTR AU-rich region binding |
| D | 0003960 | molecular_function | quinone reductase (NADPH) activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0035925 | molecular_function | mRNA 3'-UTR AU-rich region binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP A 335 |
| Chain | Residue |
| A | TYR49 |
| A | VAL161 |
| A | ALA180 |
| A | SER181 |
| A | LYS185 |
| A | SER224 |
| A | VAL225 |
| A | PHE246 |
| A | ALA249 |
| A | SER250 |
| A | ARG270 |
| A | TYR53 |
| A | PRO271 |
| A | GLN272 |
| A | LEU273 |
| A | ARG322 |
| A | GOL336 |
| A | HOH343 |
| A | HOH350 |
| A | HOH353 |
| A | HOH354 |
| A | HOH363 |
| A | LEU131 |
| A | HOH368 |
| A | HOH370 |
| A | HOH377 |
| A | HOH388 |
| A | HOH407 |
| A | HOH439 |
| A | GLN132 |
| A | THR135 |
| A | PHE139 |
| A | ALA156 |
| A | GLY159 |
| A | GLY160 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 336 |
| Chain | Residue |
| A | ILE50 |
| A | TYR53 |
| A | TYR59 |
| A | PHE246 |
| A | GLY247 |
| A | ASN248 |
| A | ARG270 |
| A | GLN272 |
| A | NDP335 |
| A | HOH743 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 337 |
| Chain | Residue |
| A | LYS305 |
| A | ASP318 |
| A | LYS323 |
| A | HOH1472 |
| B | ASN295 |
| B | LYS297 |
| site_id | AC4 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NDP B 335 |
| Chain | Residue |
| B | TYR49 |
| B | TYR53 |
| B | LEU131 |
| B | GLN132 |
| B | THR135 |
| B | PHE139 |
| B | ALA156 |
| B | GLY159 |
| B | GLY160 |
| B | VAL161 |
| B | ALA180 |
| B | SER181 |
| B | LYS185 |
| B | SER224 |
| B | VAL225 |
| B | PHE246 |
| B | GLY247 |
| B | ALA249 |
| B | ARG270 |
| B | PRO271 |
| B | GLN272 |
| B | LEU273 |
| B | ARG322 |
| B | GOL336 |
| B | HOH343 |
| B | HOH345 |
| B | HOH361 |
| B | HOH366 |
| B | HOH371 |
| B | HOH375 |
| B | HOH376 |
| B | HOH377 |
| B | HOH396 |
| B | HOH425 |
| B | HOH429 |
| B | HOH488 |
| B | HOH692 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 336 |
| Chain | Residue |
| B | ILE50 |
| B | TYR53 |
| B | TYR59 |
| B | PHE246 |
| B | GLY247 |
| B | ASN248 |
| B | ARG270 |
| B | GLN272 |
| B | NDP335 |
| B | HOH692 |
| B | HOH780 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE NDP C 335 |
| Chain | Residue |
| C | TYR49 |
| C | TYR53 |
| C | LEU131 |
| C | GLN132 |
| C | THR135 |
| C | PHE139 |
| C | ALA156 |
| C | GLY159 |
| C | GLY160 |
| C | VAL161 |
| C | ALA180 |
| C | SER181 |
| C | LYS185 |
| C | SER224 |
| C | VAL225 |
| C | PHE246 |
| C | GLY247 |
| C | ALA249 |
| C | SER250 |
| C | ARG270 |
| C | PRO271 |
| C | GLN272 |
| C | LEU273 |
| C | ILE319 |
| C | ARG322 |
| C | GOL336 |
| C | HOH338 |
| C | HOH344 |
| C | HOH358 |
| C | HOH363 |
| C | HOH368 |
| C | HOH371 |
| C | HOH372 |
| C | HOH373 |
| C | HOH379 |
| C | HOH426 |
| C | HOH822 |
| C | HOH848 |
| C | HOH950 |
| C | HOH1018 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL C 336 |
| Chain | Residue |
| C | ILE50 |
| C | TYR53 |
| C | TYR59 |
| C | PHE246 |
| C | GLY247 |
| C | ASN248 |
| C | ARG270 |
| C | GLN272 |
| C | NDP335 |
| C | HOH383 |
| C | HOH989 |
| C | HOH1018 |
| site_id | AC8 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP D 335 |
| Chain | Residue |
| D | TYR49 |
| D | TYR53 |
| D | LEU131 |
| D | GLN132 |
| D | THR135 |
| D | PHE139 |
| D | ALA156 |
| D | GLY159 |
| D | GLY160 |
| D | VAL161 |
| D | ALA180 |
| D | SER181 |
| D | LYS185 |
| D | SER224 |
| D | VAL225 |
| D | PHE246 |
| D | GLY247 |
| D | ALA249 |
| D | SER250 |
| D | ARG270 |
| D | PRO271 |
| D | GLN272 |
| D | LEU273 |
| D | ARG322 |
| D | GOL336 |
| D | HOH341 |
| D | HOH343 |
| D | HOH344 |
| D | HOH351 |
| D | HOH358 |
| D | HOH363 |
| D | HOH373 |
| D | HOH379 |
| D | HOH383 |
| D | HOH416 |
| D | HOH987 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 336 |
| Chain | Residue |
| D | ILE50 |
| D | TYR53 |
| D | TYR59 |
| D | PHE246 |
| D | GLY247 |
| D | ASN248 |
| D | ARG270 |
| D | GLN272 |
| D | NDP335 |
| D | HOH809 |
Functional Information from PROSITE/UniProt
| site_id | PS01162 |
| Number of Residues | 22 |
| Details | QOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GDyvLlfaAAGGvGlilnQllK |
| Chain | Residue | Details |
| A | GLY149-LYS170 |
