Current Protein Identity:P02696 New Search
Main Difference Dimensions in This Set
Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1CRB CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOL Deposited 1993-02-10 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–134(134 aa)
Not recorded CD CADMIUM ION × 2 RTL RETINOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å R-free 0.248
1JBH Solution structure of cellular retinol binding protein type-I in the ligand-free state Deposited 2001-06-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 0–134(135 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;298 K;Ionic strength (raw mmCIF value) 20mM POTASSIUM PHOSPHATE;Pressure AMBIENT
NMR sample composition 1.6MM CRBP-I PHOSPHATE BUFFER; 0.05% SODIUM AZIDE
Resolution not provided
1KGL Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol Deposited 2001-11-27 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 0–134(135 aa)
Not recorded RTL RETINOL × 1 SOLUTION NMR
NMR measurement conditions pH 6;298 K;Ionic strength (raw mmCIF value) 20mM POTASSIUM PHOSPHATE;Pressure AMBIENT
NMR sample composition 1.8MM CRBP-I PHOSPHATE BUFFER; 0.05% SODIUM AZIDE
Resolution not provided
1MX7 Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility Deposited 2002-10-01 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 2–135(134 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4;298 K;Ionic strength (raw mmCIF value) 0.34;Pressure ambient
NMR measurement conditions pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.34;Pressure ambient
NMR sample composition 1.0mM ligand free cellular retinol-binding protein I U-[99% 15N, 99% 13C]; 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0mM ligand free cellular retinol-binding protein I U-[99% 15N, 80% 2H]; 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0mM ligand free cellular retinol-binding protein I U-[99% 15N]; 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0mM ligand free cellular retinol-binding protein I U-[99% 15N, 99% 13C]; 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 99.5% D2O | 99.5% D2O
Resolution not provided
1MX8 Two homologous rat cellular retinol-binding proteins differ in local structure and flexibility Deposited 2002-10-01 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 2–135(134 aa)
Not recorded RTL RETINOL × 1 SOLUTION NMR
NMR measurement conditions pH 7.4;298 K;Ionic strength (raw mmCIF value) 0.34;Pressure ambient
NMR measurement conditions pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.34;Pressure ambient
NMR sample composition 1.0mM cellular retinol-binding protein I U-[99% 15N, 99% 13C] in complex with all-trans retinol (natural isotope abundance); 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0mM cellular retinol-binding protein I U-[99% 15N, 80% 2H] in complex with all-trans retinol (natural isotope abundance); 20mM phosphate buffer, 50mM potassium chloride, 0.05% sudium azide, 5mM beta-mecaptoethanol-d6; 95% H2O, 5% D2O | 95% H2O/5% D2O
Resolution not provided