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8toh

Cryo-EM structure of monomeric alpha-Klotho

Method: ELECTRON MICROSCOPY Dmax: 109.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Klotho

Homo sapiens

UniProt Q9UEF7

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 34–981 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；25mM HEPES pH7.5, 300mM NaCl, 1mM TCEP cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.29 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.

Other PDB Difference from Current Entry 8TOH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5W21 Crystal Structure of a 1:1:1 FGF23-FGFR1c-aKlotho Ternary Complex Deposited 2017-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–981（981 aa） Fragment：ectodomain (UNP residues 1-981)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；22% PEG350 MME, 0.1 M Tris-HCl, pH 8.0, 1 mM reduced glutathione, 1 mM oxidized glutathione
Resolution 3.00 Å R-free 0.278
7YSH Cryo-EM Structure of FGF23-FGFR1c-aKlotho-HS Quaternary Complex Deposited 2022-08-12 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 34–981（948 aa）
Not recorded ZN ZINC ION × 1 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.74 Å
7YSU Cryo-EM Structure of FGF23-FGFR3c-aKlotho-HS Quaternary Complex Deposited 2022-08-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 34–975（942 aa）
Not recorded ZN ZINC ION × 1 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7YSW Cryo-EM Structure of FGF23-FGFR4-aKlotho-HS Quaternary Complex Deposited 2022-08-13 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 34–975（942 aa）
Not recorded CU COPPER (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.03 Å
8UF8 Cryo-EM structure of alpha-Klotho Deposited 2023-10-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–1012（1012 aa）
Chain B 1–1012（1012 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；20mM HEPES pH7.5, 150mM NaCl, 1mM DTT
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.50 Å

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

View Construct and Data Evidence
UniProt name KLOT_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–948； UniProt 34–981

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 8toh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8toh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8toh
Deposition date deposition_date2023-08-03
Structure title titleCryo-EM structure of monomeric alpha-Klotho
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.19 Å
Radius of gyration Rg (electron density) rg_electron32.57 Å
Forward intensity I(0) i0145238000.00
Molecular weight molecular_weight99029.0 kDa
Excluded volume excluded_volume124730 ų
Envelope volume envelope_volume154270 ų
Hydration-shell volume shell_volume39880 ų
Envelope diameter envelope_diameter107.6 Å
Shell Rg shell_rg39.04 Å
Envelope Rg envelope_rg32.41 Å
Shape Rg shape_rg32.56 Å
Total Rg total_rg33.10 Å
Total atoms total_atoms7022
Residues n_residues860
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 dmax109.6 Å
Rg (real space) rg_real33.33 Å
Rg uncertainty (real space) rg_real_error0.69 Å
I(0) (real space) i0_real1.4520e+08
I(0) uncertainty (real space) i0_real_error2.2220e+06
Rg (reciprocal space) rg_reciprocal33.28 Å
I(0) (reciprocal space) i0_reciprocal145200000.0000
Solution quality estimate total_estimate0.8734
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.3 Å
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.2400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42390000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.913
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)