10nm

CRYO-EM STRUCTURE OF THE A149T DIMER VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP

Method: ELECTRON MICROSCOPY Dmax: 93.7 Å Quality: GOOD

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

Serine hydroxymethyltransferase

Glycine max

UniProt K4FZF8

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 1–471 Chain B; UniProt 1–471 Mutation:A149T Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50mM HEPES, 150mM NaCl, 0.5mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.92 Å

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.

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

View Construct and Data Evidence
UniProt name K4FZF8_SOYBN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 26–496; UniProt 1–471 Author chain B; PDBConstruct 26–496; UniProt 1–471

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 10nm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10nm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10nm
Deposition date deposition_date2026-01-28
Structure title titleCRYO-EM STRUCTURE OF THE A149T DIMER VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP
Keywords keywordsenzyme, missense variant, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.31
Radius of gyration Rg (electron density) rg_electron28.53
Forward intensity I(0) i0132826000.00
Molecular weight molecular_weight91242.0 kDa
Excluded volume excluded_volume114100 ų
Envelope volume envelope_volume143560 ų
Hydration-shell volume shell_volume41022 ų
Envelope diameter envelope_diameter98.0
Shell Rg shell_rg36.84
Envelope Rg envelope_rg28.48
Shape Rg shape_rg28.54
Total Rg total_rg29.27
Total atoms total_atoms6440
Residues n_residues895
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax93.7
Rg (real space) rg_real29.22
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.3280e+08
I(0) uncertainty (real space) i0_real_error2.0540e+06
Rg (reciprocal space) rg_reciprocal29.26
I(0) (reciprocal space) i0_reciprocal132800000.0000
Solution quality estimate total_estimate0.8977
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.418
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha58630000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)