9bvq

Vitamin K-dependent gamma-carboxylase with TMG2 propeptide and glutamate-rich region

Method: ELECTRON MICROSCOPY Dmax: 104.8 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 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–758 Not recorded Transmembrane gamma-carboxyglutamic acid protein 2 × 1 (O14669) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 1–732; UniProt 27–758

Transmembrane gamma-carboxyglutamic acid protein 2

Homo sapiens

UniProt O14669

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 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 24–139 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 × 3 6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TMG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–116; UniProt 24–139

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 9bvq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bvq
Deposition date deposition_date2024-05-20
Structure title titleVitamin K-dependent gamma-carboxylase with TMG2 propeptide and glutamate-rich region
Keywords keywords;GGCX, VKGC, Vitamin K, VKCFD, Hemophilia B, Warfarin, Carboxylation, Blood Coagulaton, Calcium homeostasis, TMG, MEMBRANE PROTEIN, Gla, LYASE-SUBSTRATE complex ;; MEMBRANE PROTEIN,LYASE/SUBSTRATE
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_electron30.45
Forward intensity I(0) i0102483000.00
Molecular weight molecular_weight84543.0 kDa
Excluded volume excluded_volume107680 ų
Envelope volume envelope_volume144890 ų
Hydration-shell volume shell_volume40064 ų
Envelope diameter envelope_diameter112.9
Shell Rg shell_rg37.28
Envelope Rg envelope_rg30.32
Shape Rg shape_rg30.42
Total Rg total_rg31.22
Total atoms total_atoms5977
Residues n_residues700
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 dmax104.8
Rg (real space) rg_real31.19
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.0250e+08
I(0) uncertainty (real space) i0_real_error1.5360e+06
Rg (reciprocal space) rg_reciprocal31.21
I(0) (reciprocal space) i0_reciprocal102500000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.321
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16990000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)