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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P00381 New Search
10PDB entries
10Biological assembly
10chain/assembly records
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
1AO8 DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE, NMR, 21 STRUCTURES Deposited 1997-07-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded MTX METHOTREXATE × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 150 mM
Resolution not provided
1BZF NMR SOLUTION STRUCTURE AND DYNAMICS OF THE COMPLEX OF LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE WITH THE NEW LIPOPHILIC ANTIFOLATE DRUG TRIMETREXATE, 22 STRUCTURES Deposited 1998-10-28 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded TMQ TRIMETREXATE × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 550 mM；Pressure 1
NMR sample composition 90% H2O/10% D2O, 100% D2O
Resolution not provided
1DIS DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH BRODIMOPRIM-4,6-DICARBOXYLATE Deposited 1995-08-01 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded BDM BRODIMOPRIM-4,6-DICARBOXYLATE × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1DIU DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH BRODIMOPRIM-4,6-DICARBOXYLATE Deposited 1995-08-01 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded BDM BRODIMOPRIM-4,6-DICARBOXYLATE × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1LUD SOLUTION STRUCTURE OF DIHYDROFOLATE REDUCTASE COMPLEXED WITH TRIMETHOPRIM AND NADPH, 24 STRUCTURES Deposited 2002-05-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 TRR 2,4-DIAMINO-5-(3,4,5-TRIMETHOXY-BENZYL)-PYRIMIDIN-1-IUM × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient
NMR sample composition 3mM DHFR-15N/TMP/NADPH, 50 mM phosphate buffer | 90% H2O/10% D2O
NMR sample composition 3 mM DHFR/TMP/NADPH, 50 mM phosphate buffer | 100% D2O
NMR sample composition 0.5mM DHFR-15N/TMP/NADPH, 50 mM phosphate buffer, 5% DMPC/DHPC (3:1) | 90% H2O/10% D2O
NMR sample composition 0.25mM DHFR-15N/TMP/NADPH, 50 mM phosphate buffer, 5% C12E5/hexanol | 90% H2O/10% D2O
Resolution not provided
2HM9 Solution structure of dihydrofolate reductase complexed with trimethoprim, 33 structures Deposited 2006-07-11 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded TRR 2,4-DIAMINO-5-(3,4,5-TRIMETHOXY-BENZYL)-PYRIMIDIN-1-IUM × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100mM KCl；Pressure ambient
NMR sample composition 0.5mM DHFR-15N/TMP, 50mM phosphate buffer, 5% DMPC/DHPC (3:1), 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM DHFR-15N/TMP, 50mM phosphate buffer, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM DHFR-15N/TMP, 50mM phosphate buffer, 100% D2O | 100% D2O
Resolution not provided
2HQP Solution structure of L.casei dihydrofolate reductase complexed with NADPH, 32 structures Deposited 2006-07-19 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100mM KCl；Pressure ambient
NMR sample composition 0.5mM DHFR-15N/NADPH, 50mM phosphate buffer, 5% DMPC/DHPC, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM DHFR-15N/NADPH, 50mM phosphate buffer, 100% H2O | 100% H2O
NMR sample composition 1mM DHFR-15N/NADPH, 50mM phosphate buffer, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2L28 Solution structure of lactobacillus casei dihydrofolate reductase apo-form, 25 conformers Deposited 2010-08-13 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–163（162 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；288 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 2 mM entity-1, 100 mM potassium chloride-2, 50 mM potassium phosphate-3, 0.1 % sodium azide-4, 100% D2O | 100% D2O
NMR sample composition 1 mM [U-99% 13C; U-99% 15N] entity-5, 100 mM potassium chloride-6, 50 mM potassium phosphate-7, 0.1 % sodium azide-8, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-99% 15N] entity-9, 100 mM potassium chloride-10, 50 mM potassium phosphate-11, 0.1 % sodium azide-12, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1 mM [U-99% 15N] entity-13, 100 mM potassium chloride-14, 50 mM potassium phosphate-15, 0.1 % sodium azide-16, 5 % DMPC/DHPC-17, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2LF1 Solution structure of L. casei dihydrofolate reductase complexed with NADPH, 30 structures Deposited 2011-06-28 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 2–163（162 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR measurement conditions pH 6.5；288 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 2 mM [U-99% 13C; U-99% 15N] DHFR, 2 mM NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 100 mM potassium chloride, 50 mM potassium phosphate, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 2 mM [U-99% 13C; U-99% 15N] DHFR, 2 mM NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 100 mM potassium chloride, 50 mM potassium phosphate, 100% D2O | 100% D2O
NMR sample composition 2 mM [U-99% 15N] DHFR, 2 mM NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 100 mM potassium chloride, 50 mM potassium phosphate, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 4 mM DHFR, 4 mM NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 100 mM potassium chloride, 50 mM potassium phosphate, 100% D2O | 100% D2O
NMR sample composition 1 mM [U-99% 15N] DHFR, 1 mM NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 100 mM potassium chloride, 50 mM potassium phosphate, 5 v/v n-octylpenta-ethylene glycol (C8E5), 1.5 v/v n-octanol, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
3DFR CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE Deposited 1982-06-25 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–162（162 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 MTX METHOTREXATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.