9l24

cryo-EM structure of Vitamin K-dependent gamma-carboxylase complexed with Matrix Gla protein

Method: ELECTRON MICROSCOPY Dmax: 103.2 Å Quality: GOOD

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

Vitamin K-dependent gamma-carboxylase

Homo sapiens

UniProt P38435

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 32–729 Not recorded Matrix Gla protein × 1 (P08493) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 A1AVC vitamin K1 hydroquinone × 1 CLR CHOLESTEROL × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 3 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VKGC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–698; UniProt 32–729

Matrix Gla protein

Homo sapiens

UniProt P08493

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 31–59 Not recorded Vitamin K-dependent gamma-carboxylase × 1 (P38435) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 A1AVC vitamin K1 hydroquinone × 1 CLR CHOLESTEROL × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 3 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name MGP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–29; UniProt 31–59

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 9l24

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9l24
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9l24
Deposition date deposition_date2024-12-16
Structure title titlecryo-EM structure of Vitamin K-dependent gamma-carboxylase complexed with Matrix Gla protein
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_guinier31.23
Radius of gyration Rg (electron density) rg_electron30.40
Forward intensity I(0) i0214085000.00
Molecular weight molecular_weight80809.0 kDa
Excluded volume excluded_volume79834 ų
Envelope volume envelope_volume149200 ų
Hydration-shell volume shell_volume41024 ų
Envelope diameter envelope_diameter108.5
Shell Rg shell_rg37.46
Envelope Rg envelope_rg30.40
Shape Rg shape_rg30.38
Total Rg total_rg30.94
Total atoms total_atoms6158
Residues n_residues704
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 dmax103.2
Rg (real space) rg_real31.21
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real2.1410e+08
I(0) uncertainty (real space) i0_real_error3.3780e+06
Rg (reciprocal space) rg_reciprocal31.22
I(0) (reciprocal space) i0_reciprocal214100000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28190000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)