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8uf8

Cryo-EM structure of alpha-Klotho

Method: ELECTRON MICROSCOPY Dmax: 139.0 Å Quality: REASONABLE
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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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–1012 Chain B； UniProt 1–1012 Not recorded No other associated polymer 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

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 8UF8 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 mutation/modification 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 construct Different mutation/modification 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 mutation/modification 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 mutation/modification 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
8TOH Cryo-EM structure of monomeric alpha-Klotho Deposited 2023-08-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 34–981（948 aa）
Not recorded No recorded non-water small molecule 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

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 1–1012； UniProt 1–1012 Author chain B； PDBConstruct 1–1012； UniProt 1–1012

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 8uf8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uf8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uf8
Deposition date deposition_date2023-10-03
Structure title titleCryo-EM structure of alpha-Klotho
Keywords keywordsprotein binding, signaling 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_guinier47.18 Å
Radius of gyration Rg (electron density) rg_electron46.53 Å
Forward intensity I(0) i0538571000.00
Molecular weight molecular_weight198060.0 kDa
Excluded volume excluded_volume249450 ų
Envelope volume envelope_volume349540 ų
Hydration-shell volume shell_volume61660 ų
Envelope diameter envelope_diameter141.7 Å
Shell Rg shell_rg53.68 Å
Envelope Rg envelope_rg44.09 Å
Shape Rg shape_rg46.54 Å
Total Rg total_rg46.81 Å
Total atoms total_atoms14044
Residues n_residues1720
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 dmax139.0 Å
Rg (real space) rg_real46.98 Å
Rg uncertainty (real space) rg_real_error0.93 Å
I(0) (real space) i0_real5.3860e+08
I(0) uncertainty (real space) i0_real_error9.5620e+06
Rg (reciprocal space) rg_reciprocal47.18 Å
I(0) (reciprocal space) i0_reciprocal538700000.0000
Solution quality estimate total_estimate0.6146
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.8 Å
Skewness Skewness skewness-0.032
Kurtosis Kurtosis kurtosis-0.956
Angular range angular_range— – 0.1650 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97450000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 0.006; Positv: 1.000; Valcen: 0.989; Smooth: 0.386
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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)