2X1H
Crystal structure of the human MGC45594 gene product in complex with raloxifene
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 | 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 |
