Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006693 | biological_process | prostaglandin metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0045599 | biological_process | negative regulation of fat cell differentiation |
A | 0047522 | molecular_function | 15-oxoprostaglandin 13-reductase [NAD(P)+] activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006693 | biological_process | prostaglandin metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0045599 | biological_process | negative regulation of fat cell differentiation |
B | 0047522 | molecular_function | 15-oxoprostaglandin 13-reductase [NAD(P)+] activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NAP A 1372 |
Chain | Residue |
A | ASN66 |
A | LYS200 |
A | TYR215 |
A | SER238 |
A | ILE260 |
A | GLY261 |
A | PHE262 |
A | ILE263 |
A | SER264 |
A | TYR266 |
A | PHE294 |
A | ALA67 |
A | LEU296 |
A | MET347 |
A | ASN352 |
A | X1H2001 |
A | HOH3042 |
A | HOH3043 |
A | HOH3134 |
A | HOH3161 |
A | HOH3169 |
A | HOH3222 |
A | THR150 |
A | HOH3226 |
A | HOH3227 |
A | HOH3303 |
A | HOH3312 |
A | HOH3313 |
A | HOH3314 |
A | ALA171 |
A | GLY174 |
A | GLY175 |
A | THR176 |
A | CYS195 |
A | SER196 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE X1H A 2001 |
Chain | Residue |
A | SER68 |
A | ASN71 |
A | ARG76 |
A | TYR77 |
A | PHE262 |
A | TYR266 |
A | THR270 |
A | LEU272 |
A | PHE295 |
A | NAP1372 |
A | HOH3315 |
A | HOH3316 |
B | LYS286 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE X1H A 2002 |
Chain | Residue |
A | TYR152 |
A | LEU155 |
A | LYS156 |
A | LEU183 |
A | LYS186 |
A | ALA187 |
A | MET313 |
A | ASP318 |
A | HOH3318 |
B | PRO269 |
B | THR270 |
site_id | AC4 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE NAP B 1372 |
Chain | Residue |
B | ALA67 |
B | THR150 |
B | ALA171 |
B | GLY174 |
B | GLY175 |
B | THR176 |
B | CYS195 |
B | SER196 |
B | LYS200 |
B | TYR215 |
B | SER238 |
B | ILE260 |
B | GLY261 |
B | PHE262 |
B | ILE263 |
B | SER264 |
B | TYR266 |
B | PHE294 |
B | LEU296 |
B | MET347 |
B | ASN352 |
B | EDO1362 |
B | X1H2001 |
B | HOH3038 |
B | HOH3039 |
B | HOH3103 |
B | HOH3126 |
B | HOH3142 |
B | HOH3190 |
B | HOH3256 |
B | HOH3257 |
B | HOH3258 |
B | HOH3259 |
B | HOH3260 |
B | HOH3261 |
B | HOH3262 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE X1H B 2001 |
Chain | Residue |
B | TYR266 |
B | THR270 |
B | LEU272 |
B | PHE295 |
B | EDO1362 |
B | NAP1372 |
B | HOH3194 |
B | HOH3263 |
B | SER68 |
B | ASN71 |
B | ARG76 |
B | TYR77 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE X1H B 2002 |
Chain | Residue |
B | ALA151 |
B | TYR152 |
B | LEU155 |
B | LYS156 |
B | LEU183 |
B | LYS186 |
B | ALA187 |
B | HIS309 |
B | HOH3128 |
B | HOH3264 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 1362 |
Chain | Residue |
A | GLY159 |
A | GLY160 |
A | LYS165 |
A | ASP233 |
A | VAL234 |
A | HOH3200 |
A | HOH3217 |
A | HOH3307 |
A | HOH3308 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1363 |
Chain | Residue |
A | PRO135 |
A | HOH3269 |
A | HOH3310 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1364 |
Chain | Residue |
A | ARG342 |
A | ASN345 |
A | TYR346 |
A | MET349 |
A | HOH3311 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1362 |
Chain | Residue |
B | SER68 |
B | VAL146 |
B | NAP1372 |
B | X1H2001 |
B | HOH3040 |
Functional Information from PROSITE/UniProt
site_id | PS01162 |
Number of Residues | 22 |
Details | QOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GKkvLvtaAAGGtGqfamQlsK |
Chain | Residue | Details |
A | GLY164-LYS185 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|Ref.9 |
Chain | Residue | Details |
A | THR176 | |
B | THR176 | |
B | SER196 | |
B | LYS200 | |
B | TYR215 | |
B | SER238 | |
B | ILE260 | |
B | TYR266 | |
B | PHE294 | |
B | ASN352 | |
A | SER196 | |
A | LYS200 | |
A | TYR215 | |
A | SER238 | |
A | ILE260 | |
A | TYR266 | |
A | PHE294 | |
A | ASN352 | |
Chain | Residue | Details |
A | LYS26 | |
B | LYS26 | |
Chain | Residue | Details |
A | SER290 | |
B | SER290 | |