9mnz

Cryo-EM structure of human MPC in complex with UK5099 in nanodiscs

Method: ELECTRON MICROSCOPY Dmax: 138.2 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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–127 Not recorded Fab_8D3_2 heavy chain × 1 Nanobody × 1 Mitochondrial pyruvate carrier 1 × 1 (Q9Y5U8) MBP-PrA/G × 1 Fab_8D3_2 light chain × 1 I2R (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.73 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 3
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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–109 Not recorded Fab_8D3_2 heavy chain × 1 Nanobody × 1 Mitochondrial pyruvate carrier 2 × 1 (O95563) MBP-PrA/G × 1 Fab_8D3_2 light chain × 1 I2R (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.73 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 4
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 9mnz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mnz
Deposition date deposition_date2024-12-24
Structure title titleCryo-EM structure of human MPC in complex with UK5099 in nanodiscs
Keywords keywordsMembrane transporter, TRANSPORT PROTEIN-IMMUNE SYSTEM complex; TRANSPORT PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.58
Radius of gyration Rg (electron density) rg_electron40.43
Forward intensity I(0) i089657400.00
Molecular weight molecular_weight76357.0 kDa
Excluded volume excluded_volume95560 ų
Envelope volume envelope_volume150960 ų
Hydration-shell volume shell_volume32687 ų
Envelope diameter envelope_diameter140.6
Shell Rg shell_rg43.49
Envelope Rg envelope_rg39.91
Shape Rg shape_rg40.47
Total Rg total_rg40.51
Total atoms total_atoms5379
Residues n_residues682
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 dmax138.2
Rg (real space) rg_real40.14
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real8.9660e+07
I(0) uncertainty (real space) i0_real_error1.8220e+06
Rg (reciprocal space) rg_reciprocal39.81
I(0) (reciprocal space) i0_reciprocal89630000.0000
Solution quality estimate total_estimate0.7044
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.723
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5995000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.568; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.451; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)