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8skr

human liver mitochondrial Aspartate aminotransferase

Method: ELECTRON MICROSCOPY Dmax: 99.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Aspartate aminotransferase, mitochondrial

OrganismNot specified

UniProt P00505

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 1–430 Chain C； UniProt 1–430 Not recorded PLP PYRIDOXAL-5'-PHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.99 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 8SKR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5AX8 Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase Deposited 2015-07-20 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 30–430（401 aa） Fragment：UNP residues 40-430
Chain C 30–430（401 aa） Fragment：UNP residues 40-430
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；0.1 M HEPES pH 6.8, 25% (v/v) Jeffamine ED-2001 pH 6.8
Resolution 2.99 Å R-free 0.291
5AX8 Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase Deposited 2015-07-20 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 30–430（401 aa） Fragment：UNP residues 40-430
Chain D 30–430（401 aa） Fragment：UNP residues 40-430
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277 K；0.1 M HEPES pH 6.8, 25% (v/v) Jeffamine ED-2001 pH 6.8
Resolution 2.99 Å R-free 0.291
9YB6 Human Mitochondrial Aspartate Aminotransferase complex with PLP at 1.5 Angstrom. Deposited 2025-09-16 Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–430（430 aa）
Chain B 1–430（430 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GOL GLYCEROL × 5 SO4 SULFATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Ammonium Sulfate, 0.05 M Sodium Acetate, 23% PEG-3350, pH 5.5
Resolution 1.50 Å R-free 0.209

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

View Construct and Data Evidence
UniProt name AATM_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–430； UniProt 1–430 Author chain C； PDBConstruct 1–430； UniProt 1–430

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 8skr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8skr
Deposition date deposition_date2023-04-20
Structure title titlehuman liver mitochondrial Aspartate aminotransferase
Keywords keywordshuman, liver, mitochondrial, Aspartate aminotransferase, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.36 Å
Radius of gyration Rg (electron density) rg_electron28.48 Å
Forward intensity I(0) i0128748000.00
Molecular weight molecular_weight90007.0 kDa
Excluded volume excluded_volume112750 ų
Envelope volume envelope_volume135280 ų
Hydration-shell volume shell_volume39139 ų
Envelope diameter envelope_diameter105.9 Å
Shell Rg shell_rg36.16 Å
Envelope Rg envelope_rg28.61 Å
Shape Rg shape_rg28.48 Å
Total Rg total_rg29.18 Å
Total atoms total_atoms6332
Residues n_residues804
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 dmax99.8 Å
Rg (real space) rg_real29.33 Å
Rg uncertainty (real space) rg_real_error0.58 Å
I(0) (real space) i0_real1.2870e+08
I(0) uncertainty (real space) i0_real_error1.8020e+06
Rg (reciprocal space) rg_reciprocal29.34 Å
I(0) (reciprocal space) i0_reciprocal128700000.0000
Solution quality estimate total_estimate0.6674
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.1 Å
Skewness Skewness skewness0.358
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha70490000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 0.092; Positv: 1.000; Valcen: 0.998; Smooth: 0.978
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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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8. Citations (1)

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9. Files and Curves (10)