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. Author manuscript; available in PMC: 2013 Jan 30.
Published in final edited form as: J Comput Chem. 2011 Nov 23;33(3):301–310. doi: 10.1002/jcc.21978

Table 1.

Retinoic acid (RA) entries in the PDB

A. All-trans retinoic acid entries in the PDB
PDB ID Resolution (Å) Protein Description R/Rfree SF
1CBR 2.90 Holo cellular RA-binding protein type I 0.251/0.320
1CBS 1.80 Holo cellular RA-binding protein type II 0.200/0.237
1EPB 2.20 Epididymal RA-binding protein 0.182 N/A
1FEM 1.90 Bovine plasma retinol-binding protein 0.184 N/A
1GX9 2.34 Bovine β-lactoglobulin 0.226/0.298 N/A
1N4H 2.10 Orphan nuclear receptor ROR-β 0.217/0.255 N/A
1RLB 3.10 Transthyretin and retinol-binding protein 0.215 N/A
2FR3 1.48 Apo-wild-type cellular RA-binding protein type II 0.131/0.174 N/A
2G78 1.70 The R132K:Y134F mutant of cellular RA-Binding protein type II 0.151/0.203 N/A
2LBD 2.06 Ligand-binding domain of the human RAR-γ 0.210/0.313
2VE3 2.10 Cyanobacterial cytochrome P450 CYP120A1 0.225/0.267
3CWK 1.60 Cellular RA-binding protein type II-R132K:Y134F:R111L:L121E:T54V 0.125/0.167
B. 9-cis retinoic acid entries in the PDB
PDB ID Resolution (Å) Protein Description R/Rfree SF
1FBY 2.25 Human RXR-α ligand binding domain 0.228/0.263 N/A
1FM6 2.10 Human RXR-α and PPAR-γ ligand binding domain 0.250/0.292
1FM9 2.10 Human RXR-α and PPAR-γ ligand binding domain 0.239/0.268
1G5Y 2.00 RXR-α ligand binding domain 0.231/0.254 N/A
1K74 2.30 Human RXR-α and PPAR-γ ligand binding domain 0.238/0.279 N/A
1TYR 1.80 Transthyretin 0.196 N/A
1XDK 2.90 RAR-β/RXR-α ligand binding domain 0.253/0.296
2ACL 2.80 Liver X receptor agonists 0.220/0.280
2NNH 2.60 Cytochrome P450 0.172/0.267
3LBD 2.40 Human nuclear receptor RAR-γ 0.210/0.313 N/A
3DZU 3.20 PAR-γ-RXR-α nuclear receptor complex on DNA 0.201/0.272
3DZY 3.10 PAR-γ-RXR-α nuclear receptor complex on DNA 0.213/0.268