6wv7

Human VKOR with Chlorophacinone

Method: X-RAY DIFFRACTION Dmax: 124.2 Å Quality: GOOD

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

Vitamin K epoxide reductase, termini restrained by green fluorescent protein

Aequorea victoria

UniProt A0A059PIQ0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–144 Chain A; UniProt 146–231 Fragment:GPF (UNP residues 1-144) + VKOR + GFP (UNP residues 146-231) Non-standard monomer:Yes (specific site not provided by mmCIF) UAJ Chlorophacinone × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;33% PEG400, 5% DMSO, 0.1 M sodium acetate, 0.1 M MES, pH 6.5 Resolution 2.48 Å R-free 0.245
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–144 Chain B; UniProt 146–231 Fragment:GPF (UNP residues 1-144) + VKOR + GFP (UNP residues 146-231) Non-standard monomer:Yes (specific site not provided by mmCIF) UAJ Chlorophacinone × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;33% PEG400, 5% DMSO, 0.1 M sodium acetate, 0.1 M MES, pH 6.5 Resolution 2.48 Å R-free 0.245

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.

91 other PDB entries and 136 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–142; UniProt 1–144 Author chain A; PDBConstruct 296–381; UniProt 146–231 Author chain B; PDBConstruct 1–142; UniProt 1–144 Author chain B; PDBConstruct 296–381; UniProt 146–231

Vitamin K epoxide reductase, termini restrained by green fluorescent protein

Aequorea victoria

UniProt Q9BQB6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–155 Fragment:GPF (UNP residues 1-144) + VKOR + GFP (UNP residues 146-231) Non-standard monomer:Yes (specific site not provided by mmCIF) UAJ Chlorophacinone × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;33% PEG400, 5% DMSO, 0.1 M sodium acetate, 0.1 M MES, pH 6.5 Resolution 2.48 Å R-free 0.245
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–155 Fragment:GPF (UNP residues 1-144) + VKOR + GFP (UNP residues 146-231) Non-standard monomer:Yes (specific site not provided by mmCIF) UAJ Chlorophacinone × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;33% PEG400, 5% DMSO, 0.1 M sodium acetate, 0.1 M MES, pH 6.5 Resolution 2.48 Å R-free 0.245

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VKOR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 143–295; UniProt 3–155 Author chain B; PDBConstruct 143–295; UniProt 3–155

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 6wv7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wv7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wv7
Deposition date deposition_date2020-05-05
Structure title titleHuman VKOR with Chlorophacinone
Keywords keywords;Vitamin K epoxide Reductase (VKOR), Vitamin K, warfarin, superwarfarin, vitamin K expoxide(KO), Chlorophacinone, membrane protein, OXIDOREDUCTASE, FLUORESCENT PROTEIN ;; OXIDOREDUCTASE, FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.20
Radius of gyration Rg (electron density) rg_electron37.82
Forward intensity I(0) i0112623000.00
Molecular weight molecular_weight87397.0 kDa
Excluded volume excluded_volume110050 ų
Envelope volume envelope_volume150660 ų
Hydration-shell volume shell_volume34861 ų
Envelope diameter envelope_diameter134.2
Shell Rg shell_rg41.73
Envelope Rg envelope_rg37.00
Shape Rg shape_rg37.85
Total Rg total_rg37.99
Total atoms total_atoms6198
Residues n_residues768
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 dmax124.2
Rg (real space) rg_real38.54
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real1.1260e+08
I(0) uncertainty (real space) i0_real_error2.1390e+06
Rg (reciprocal space) rg_reciprocal38.34
I(0) (reciprocal space) i0_reciprocal112600000.0000
Solution quality estimate total_estimate0.8158
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6031000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.833; Smooth: 0.085

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6wv7A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily130 — VKOR domain
Domain ID domain_id6wv7B01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily130 — VKOR domain

8. Citations (1)

9. Files and Curves (10)