8yw6

Cryo-EM structure of apo human mitochondrial pyruvate carrier in the IMS-open conformation at pH 8.0

Method: ELECTRON MICROSCOPY Dmax: 101.3 Å Quality: GOOD

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–127 Not recorded MPC specific nanobody 1 × 1 Mitochondrial pyruvate carrier 1 × 1 (Q9Y5U8) PC8 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 CDL CARDIOLIPIN × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 1–127; UniProt 1–127

Mitochondrial pyruvate carrier 1

Homo sapiens

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 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–109 Not recorded Mitochondrial pyruvate carrier 2 × 1 (O95563) MPC specific nanobody 1 × 1 PC8 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 CDL CARDIOLIPIN × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 3
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 8yw6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yw6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yw6
Deposition date deposition_date2024-03-29
Structure title titleCryo-EM structure of apo human mitochondrial pyruvate carrier in the IMS-open conformation at pH 8.0
Keywords keywordsmitochondrial pyruvate carrier, MPC, pyruvate transport, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.84
Radius of gyration Rg (electron density) rg_electron27.17
Forward intensity I(0) i023620300.00
Molecular weight molecular_weight39064.0 kDa
Excluded volume excluded_volume49680 ų
Envelope volume envelope_volume62981 ų
Hydration-shell volume shell_volume21211 ų
Envelope diameter envelope_diameter105.1
Shell Rg shell_rg31.53
Envelope Rg envelope_rg27.83
Shape Rg shape_rg27.15
Total Rg total_rg27.77
Total atoms total_atoms2747
Residues n_residues333
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 dmax101.3
Rg (real space) rg_real28.17
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real2.3620e+07
I(0) uncertainty (real space) i0_real_error3.9150e+05
Rg (reciprocal space) rg_reciprocal28.07
I(0) (reciprocal space) i0_reciprocal23620000.0000
Solution quality estimate total_estimate0.7999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.486
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3020000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.650; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.449; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)