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 | NADPH:quinone reductase 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 |
A | 0070402 | molecular_function | NADPH binding |
B | 0003960 | molecular_function | NADPH:quinone reductase 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 |
B | 0070402 | molecular_function | NADPH binding |
C | 0003960 | molecular_function | NADPH:quinone reductase 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 |
C | 0070402 | molecular_function | NADPH binding |
D | 0003960 | molecular_function | NADPH:quinone reductase 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 |
D | 0070402 | molecular_function | NADPH 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 |