2X7H
Crystal structure of the human MGC45594 gene product in complex with fenoprofen
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 | 9 |
| Details | BINDING SITE FOR RESIDUE PFN A 1372 |
| Chain | Residue |
| A | TYR161 |
| A | LEU192 |
| A | HIS318 |
| A | EDO1380 |
| A | HOH2222 |
| A | HOH2223 |
| B | THR277 |
| B | LEU281 |
| B | PRO283 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP A 1373 |
| Chain | Residue |
| A | ALA76 |
| A | THR159 |
| A | ALA180 |
| A | GLY183 |
| A | GLY184 |
| A | THR185 |
| A | CYS204 |
| A | SER205 |
| A | LYS209 |
| A | TYR224 |
| A | SER247 |
| A | VAL248 |
| A | ILE269 |
| A | GLY270 |
| A | PHE271 |
| A | ILE272 |
| A | SER273 |
| A | TYR275 |
| A | PHE303 |
| A | LEU305 |
| A | MET356 |
| A | ASN361 |
| A | PFN1375 |
| A | HOH2029 |
| A | HOH2030 |
| A | HOH2084 |
| A | HOH2099 |
| A | HOH2145 |
| A | HOH2207 |
| A | HOH2214 |
| A | HOH2215 |
| A | HOH2216 |
| A | HOH2217 |
| A | HOH2218 |
| A | HOH2219 |
| A | HOH2220 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PFN A 1374 |
| Chain | Residue |
| A | PRO144 |
| A | SER145 |
| A | LYS147 |
| A | TYR150 |
| A | CYS323 |
| A | EDO1381 |
| A | HOH2221 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PFN A 1375 |
| Chain | Residue |
| A | SER77 |
| A | TYR86 |
| A | VAL155 |
| A | TYR275 |
| A | NAP1373 |
| A | HOH2213 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PFN A 1376 |
| Chain | Residue |
| A | VAL143 |
| A | PRO144 |
| A | LEU320 |
| A | GLU321 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1377 |
| Chain | Residue |
| A | GLY168 |
| A | GLY169 |
| A | LYS174 |
| A | ASP242 |
| A | LYS263 |
| A | HOH2224 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1378 |
| Chain | Residue |
| A | HOH2225 |
| A | HOH2226 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1379 |
| Chain | Residue |
| A | PHE271 |
| A | LEU281 |
| A | SER282 |
| A | HOH2227 |
| B | GLY287 |
| B | THR288 |
| B | PRO290 |
| B | ALA291 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1380 |
| Chain | Residue |
| A | PFN1372 |
| A | HOH2087 |
| A | HOH2228 |
| B | THR277 |
| B | PRO278 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1381 |
| Chain | Residue |
| A | SER145 |
| A | LYS147 |
| A | PRO278 |
| A | PFN1374 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1382 |
| Chain | Residue |
| A | TYR81 |
| A | GLY84 |
| A | ARG85 |
| A | TYR86 |
| A | ASP87 |
| A | PHE94 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1383 |
| Chain | Residue |
| A | HOH2230 |
| A | PRO43 |
| A | ASN44 |
| A | PHE45 |
| A | GLN276 |
| A | ASN354 |
| A | HOH2229 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1384 |
| Chain | Residue |
| A | GLY230 |
| A | LEU233 |
| A | LYS234 |
| A | TYR237 |
| A | ALA259 |
| A | HOH2231 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1385 |
| Chain | Residue |
| A | PHE253 |
| A | ASP254 |
| A | VAL257 |
| A | ASP258 |
| A | LYS285 |
| A | ALA286 |
| A | LYS292 |
| A | HOH2232 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PFN B 1372 |
| Chain | Residue |
| B | SER77 |
| B | TYR86 |
| B | VAL155 |
| B | TYR275 |
| B | NAP1373 |
| B | HOH2168 |
| site_id | BC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP B 1373 |
| Chain | Residue |
| B | ASN75 |
| B | ALA76 |
| B | THR159 |
| B | ALA180 |
| B | GLY183 |
| B | GLY184 |
| B | THR185 |
| B | CYS204 |
| B | SER205 |
| B | LYS209 |
| B | TYR224 |
| B | SER247 |
| B | VAL248 |
| B | ILE269 |
| B | GLY270 |
| B | PHE271 |
| B | ILE272 |
| B | SER273 |
| B | TYR275 |
| B | PHE303 |
| B | LEU305 |
| B | MET356 |
| B | ASN361 |
| B | PFN1372 |
| B | HOH2017 |
| B | HOH2018 |
| B | HOH2057 |
| B | HOH2071 |
| B | HOH2110 |
| B | HOH2164 |
| B | HOH2169 |
| B | HOH2170 |
| B | HOH2171 |
| B | HOH2172 |
| B | HOH2173 |
| B | HOH2174 |
| B | HOH2175 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PFN B 1374 |
| Chain | Residue |
| B | TYR161 |
| B | LEU192 |
| B | HIS318 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 1375 |
| Chain | Residue |
| B | GLY168 |
| B | GLY169 |
| B | LYS174 |
| B | ASP242 |
| B | VAL243 |
| B | LYS263 |
| B | HOH2176 |
| B | HOH2177 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1376 |
| Chain | Residue |
| B | GLN191 |
| B | LYS194 |
| B | LYS195 |
| B | LEU216 |
| B | HOH2072 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1377 |
| Chain | Residue |
| B | PRO43 |
| B | ASN44 |
| B | PHE45 |
| B | GLN276 |
| B | ASN354 |
| B | HOH2178 |
| B | HOH2179 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1378 |
| Chain | Residue |
| B | MET252 |
| B | LEU255 |
| B | HOH2180 |
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 | GLY173-LYS194 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2005","submissionDatabase":"PDB data bank","title":"The structure of MGC45594 gene product.","authors":["Bunkoczi G.","Shafqat N.","Guo K.","Smee C.","Arrowsmith C.","Edwards A.","Weigelt J.","Sundstrom M.","Gileadi O.","Von Delft F.","Oppermann U."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BGC4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
