9bum

Structure of gamma-glutamyl carboxylase (GGCX)

Method: ELECTRON MICROSCOPY Dmax: 100.1 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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–758 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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 1–758; UniProt 1–758

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 9bum

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bum
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bum
Deposition date deposition_date2024-05-17
Structure title titleStructure of gamma-glutamyl carboxylase (GGCX)
Keywords keywordsvitamin K cycle, MEMBRANE PROTEIN, LYASE; MEMBRANE PROTEIN,LYASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.34
Radius of gyration Rg (electron density) rg_electron29.48
Forward intensity I(0) i057534300.00
Molecular weight molecular_weight62493.0 kDa
Excluded volume excluded_volume79485 ų
Envelope volume envelope_volume103770 ų
Hydration-shell volume shell_volume30586 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg35.25
Envelope Rg envelope_rg29.52
Shape Rg shape_rg29.45
Total Rg total_rg30.20
Total atoms total_atoms4415
Residues n_residues538
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 dmax100.1
Rg (real space) rg_real30.44
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real5.7530e+07
I(0) uncertainty (real space) i0_real_error9.7600e+05
Rg (reciprocal space) rg_reciprocal30.40
I(0) (reciprocal space) i0_reciprocal57530000.0000
Solution quality estimate total_estimate0.8886
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.364
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8403000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.901; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)