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1b0a

5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI.

Method: X-RAY DIFFRACTION Dmax: 64.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (FOLD BIFUNCTIONAL PROTEIN)

Escherichia coli K12

UniProt P24186

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–288 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5 Resolution 2.56 Å R-free 0.292

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 1B0A Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5O22 E. coli FolD in complex with carolacton Deposited 2017-05-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–288（287 aa）
Chain B 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) C3R Carolacton × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 and 30 % (w/v) PEG 8000
Resolution 2.10 Å R-free 0.206
5O22 E. coli FolD in complex with carolacton Deposited 2017-05-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 2–288（287 aa）
Chain D 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) C3R Carolacton × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 and 30 % (w/v) PEG 8000
Resolution 2.10 Å R-free 0.206
5O28 E. coli FolD apo Deposited 2017-05-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–288（287 aa）
Chain B 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 and 30 % (w/v) PEG 8000
Resolution 1.89 Å R-free 0.209
5O28 E. coli FolD apo Deposited 2017-05-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 2–288（287 aa）
Chain D 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 and 30 % (w/v) PEG 8000
Resolution 1.89 Å R-free 0.209
5O2A FolD Q98H Deposited 2017-05-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–288（287 aa）
Chain B 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 Ammonium Sulfate, Bis-Tris pH 6.0 and 25 % PEG 3350
Resolution 1.90 Å R-free 0.181
5O2A FolD Q98H Deposited 2017-05-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 2–288（287 aa）
Chain D 2–288（287 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 Ammonium Sulfate, Bis-Tris pH 6.0 and 25 % PEG 3350
Resolution 1.90 Å R-free 0.181

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FOLD_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–288； UniProt 1–288

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1b0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b0a
Deposition date deposition_date1998-11-06
Structure title title5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI.
Keywords keywordsFOLATE, DEHYDROGENASE, CYCLCOHYDROLASE, BIFUNCTIONAL, CHANNELING, OXIDOREDUCTASE, HYDROLASE; OXIDOREDUCTASE,HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.89 Å
Radius of gyration Rg (electron density) rg_electron19.73 Å
Forward intensity I(0) i016635600.00
Molecular weight molecular_weight30908.0 kDa
Excluded volume excluded_volume38856 ų
Envelope volume envelope_volume47205 ų
Hydration-shell volume shell_volume20138 ų
Envelope diameter envelope_diameter66.1 Å
Shell Rg shell_rg25.88 Å
Envelope Rg envelope_rg19.85 Å
Shape Rg shape_rg19.76 Å
Total Rg total_rg20.53 Å
Total atoms total_atoms2173
Residues n_residues287
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax64.2 Å
Rg (real space) rg_real20.81 Å
Rg uncertainty (real space) rg_real_error0.30 Å
I(0) (real space) i0_real1.6640e+07
I(0) uncertainty (real space) i0_real_error2.1570e+05
Rg (reciprocal space) rg_reciprocal20.83 Å
I(0) (reciprocal space) i0_reciprocal16640000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1 Å
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.443
Angular range angular_range— – 0.3800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2335000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.994
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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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1b0aa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.7 — Aminoacid dehydrogenase-like, C-terminal domain
Domain ID domain_idd1b0aa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.58 — Aminoacid dehydrogenase-like, N-terminal domain
Superfamily Superfamily superfamilyc.58.1 — Aminoacid dehydrogenase-like, N-terminal domain
Family Family familyc.58.1.2 — Tetrahydrofolate dehydrogenase/cyclohydrolase

CATH v4.4 (2 domains)

Domain ID domain_id1b0aA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1b0aA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10860 — Leucine Dehydrogenase, chain A, domain 1
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8. Citations (1)

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9. Files and Curves (10)