SAXSdb — 1ao8

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1. Protein Identity and Related Structures Protein Identity & Related Structures

DIHYDROFOLATE REDUCTASE

Lactobacillus casei

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–162	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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1AO8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different construct Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DYR_LACCA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–162； UniProt 1–162

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ao8
Deposition date deposition_date	1997-07-22
Structure title title	DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE, NMR, 21 STRUCTURES
Keywords keywords	OXIDOREDUCTASE, INHIBITOR-ENZYME COMPLEX; OXIDOREDUCTASE
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	16.36 Å
Radius of gyration Rg (electron density) rg_electron	15.84 Å
Forward intensity I(0) i0	2130750000.00
Molecular weight molecular_weight	393900.0 kDa
Excluded volume excluded_volume	492320 Å³
Envelope volume envelope_volume	36583 Å³
Hydration-shell volume shell_volume	17785 Å³
Envelope diameter envelope_diameter	54.9 Å
Shell Rg shell_rg	23.44 Å
Envelope Rg envelope_rg	17.32 Å
Shape Rg shape_rg	15.82 Å
Total Rg total_rg	15.99 Å
Total atoms total_atoms	54831
Residues n_residues	3402
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	49.5 Å
Rg (real space) rg_real	16.26 Å
Rg uncertainty (real space) rg_real_error	0.19 Å
I(0) (real space) i0_real	2.1310e+09
I(0) uncertainty (real space) i0_real_error	2.2490e+07
Rg (reciprocal space) rg_reciprocal	16.27 Å
I(0) (reciprocal space) i0_reciprocal	2131000000.0000
Solution quality estimate total_estimate	0.9012
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.6 Å
Skewness Skewness skewness	0.132
Kurtosis Kurtosis kurtosis	-0.400
Angular range angular_range	— – 0.4850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	800900.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.958

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ao8a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.71 — Dihydrofolate reductase-like
Superfamily Superfamily superfamily	c.71.1 — Dihydrofolate reductase-like
Family Family family	c.71.1.1 — Dihydrofolate reductases

CATH v4.4 (1 domains)

Domain ID domain_id	1ao8A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	430 — Dihydrofolate Reductase, subunit A
Homologous superfamily homologous superfamily	10 — Dihydrofolate Reductase, subunit A

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8. Citations (2)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	DIHYDROFOLATE REDUCTASE
Molecular weight formula_weight	18331.6 kDa
EC 编号 ec_number	1.5.1.3
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	54831

来源生物 organism	Lactobacillus casei
NCBI Class编号 ncbi_taxonomy_id	1582
宿主生物 host_organism	Escherichia coli

DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE, NMR, 21 STRUCTURES

1. Protein Identity and Related Structures Protein Identity & Related Structures

DIHYDROFOLATE REDUCTASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	METHOTREXATE
Molecular weight formula_weight	454.4 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/ao/1ao8/1ao8.fit
pddf	/app/data/pr_computation/ao/1ao8/1ao8.pr.out
profile	/app/data/saxs_computation/ao/1ao8/1ao8.dat