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6xmo

Human aldolase A I98F

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fructose-bisphosphate aldolase A

Homo sapiens

UniProt P04075

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–364 Chain B； UniProt 1–364 Mutation：I98F PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.75；277 K；12% (w/v) PEG 8000, 15% (v/v) glycerol, 0.04 M potassium phosphate, pH 5.75 Resolution 2.60 Å R-free 0.259

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 6XMO Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ALD ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES Deposited 1991-05-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–363（363 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
2ALD HUMAN MUSCLE ALDOLASE Deposited 1998-10-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–363（363 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.10 Å R-free 0.258
4ALD HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE Deposited 1998-07-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–363（363 aa）
Not recorded 2FP 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM) × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.80 Å R-free 0.304
5KY6 Human muscle fructose-1,6-bisphosphate aldolase Deposited 2016-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–364（363 aa）
Chain B 2–364（363 aa）
Chain C 2–364（363 aa）
Chain D 2–364（363 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；1.6M ammonium citrate tribasic
Resolution 1.94 Å R-free 0.223
6XMH Human aldolase A wild type Deposited 2020-06-30 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–364（364 aa）
Chain B 1–364（364 aa）
Not recorded PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.75；277 K；10% (w/v) PEG 8,000, 18% (v/v) glycerol, 0.04 M potassium phosphate, pH 5.75
Resolution 1.95 Å R-free 0.286
6XML Human aldolase A I98C Deposited 2020-06-30 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–364（364 aa）
Chain B 1–364（364 aa）
Mutation：I98C Mutation：I98C PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；10% (w/v) PEG 8000, 21% (v/v) glycerol in 0.04 M potassium phosphate, pH 6.0
Resolution 1.88 Å R-free 0.286
6XMM Human aldolase A I98S Deposited 2020-06-30 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–364（364 aa）
Chain B 1–364（364 aa）
Mutation：I98S Mutation：I98S PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；10% (w/v) PEG 8000, 15% (v/v) glycerol, 0.04 M potassium phosphate, pH 6.0
Resolution 2.11 Å R-free 0.295

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ALDOA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–364； UniProt 1–364 Author chain B； PDBConstruct 1–364； UniProt 1–364

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 6xmo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xmo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xmo
Deposition date deposition_date2020-06-30
Structure title titleHuman aldolase A I98F
Keywords keywordsrheostat, allosterism, LYASE; LYASE
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_guinier28.84 Å
Radius of gyration Rg (electron density) rg_electron28.10 Å
Forward intensity I(0) i097378600.00
Molecular weight molecular_weight77452.0 kDa
Excluded volume excluded_volume96785 ų
Envelope volume envelope_volume112050 ų
Hydration-shell volume shell_volume33657 ų
Envelope diameter envelope_diameter103.5 Å
Shell Rg shell_rg34.82 Å
Envelope Rg envelope_rg28.37 Å
Shape Rg shape_rg28.13 Å
Total Rg total_rg28.59 Å
Total atoms total_atoms10908
Residues n_residues706
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 dmax98.0 Å
Rg (real space) rg_real28.95 Å
Rg uncertainty (real space) rg_real_error0.71 Å
I(0) (real space) i0_real9.7380e+07
I(0) uncertainty (real space) i0_real_error1.2950e+06
Rg (reciprocal space) rg_reciprocal28.91 Å
I(0) (reciprocal space) i0_reciprocal97380000.0000
Solution quality estimate total_estimate0.8539
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3 Å
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.218
Angular range angular_range— – 0.2750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26720000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.905
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6xmoa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.10 — Aldolase
Family Family familyc.1.10.1 — Class I aldolase
Domain ID domain_idd6xmob_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.10 — Aldolase
Family Family familyc.1.10.1 — Class I aldolase
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8. Citations (1)

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9. Files and Curves (10)