9o9t

Structure of human MPC IMS-open

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: REASONABLE

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

Mitochondrial pyruvate carrier 2

Homo sapiens

UniProt O95563

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–124 Not recorded Mitochondrial pyruvate carrier 1/MBP chimera protein × 1 (Q9Y5U8,P0AEX9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MPC2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–124; UniProt 1–124

Mitochondrial pyruvate carrier 1/MBP chimera protein

Escherichia coli K-12

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 29–384 Not recorded Mitochondrial pyruvate carrier 2 × 1 (O95563) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 125–480; UniProt 29–384

Mitochondrial pyruvate carrier 1/MBP chimera protein

Escherichia coli K-12

UniProt Q9Y5U8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–109 Not recorded Mitochondrial pyruvate carrier 2 × 1 (O95563) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.31 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MPC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–109; UniProt 1–109

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 9o9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o9t
Deposition date deposition_date2025-04-18
Structure title titleStructure of human MPC IMS-open
Keywords keywordsMEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.02
Radius of gyration Rg (electron density) rg_electron34.13
Forward intensity I(0) i079469400.00
Molecular weight molecular_weight73887.0 kDa
Excluded volume excluded_volume93600 ų
Envelope volume envelope_volume124750 ų
Hydration-shell volume shell_volume31693 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg39.07
Envelope Rg envelope_rg33.54
Shape Rg shape_rg34.13
Total Rg total_rg34.53
Total atoms total_atoms5222
Residues n_residues674
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 dmax108.8
Rg (real space) rg_real34.08
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real7.9470e+07
I(0) uncertainty (real space) i0_real_error1.3830e+06
Rg (reciprocal space) rg_reciprocal34.05
I(0) (reciprocal space) i0_reciprocal79470000.0000
Solution quality estimate total_estimate0.6973
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.782
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha13020000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 0.214; Positv: 1.000; Valcen: 0.842; Smooth: 0.875

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)