6wv4

Human VKOR C43S with warfarin

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: GOOD

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

Vitamin K epoxide reductase Cys43Ser mutant, 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) Mutation:C43S Non-standard monomer:Yes (specific site not provided by mmCIF) SWF S-WARFARIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;25-33% PEG400, 185-220 mM potassium formate, 0.1 M MES, pH 6.5 Resolution 3.01 Å R-free 0.292

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 137 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

Vitamin K epoxide reductase Cys43Ser mutant, 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) Mutation:C43S Non-standard monomer:Yes (specific site not provided by mmCIF) SWF S-WARFARIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;pH 6.5;295 K;25-33% PEG400, 185-220 mM potassium formate, 0.1 M MES, pH 6.5 Resolution 3.01 Å R-free 0.292

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 7 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

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 6wv4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wv4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wv4
Deposition date deposition_date2020-05-05
Structure title titleHuman VKOR C43S with warfarin
Keywords keywords;Vitamin K epoxide Reductase (VKOR), Vitamin K, warfarin, superwarfarin, vitamin K expoxide(KO), 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_guinier26.85
Radius of gyration Rg (electron density) rg_electron26.64
Forward intensity I(0) i026823500.00
Molecular weight molecular_weight41073.0 kDa
Excluded volume excluded_volume51914 ų
Envelope volume envelope_volume64796 ų
Hydration-shell volume shell_volume21964 ų
Envelope diameter envelope_diameter90.1
Shell Rg shell_rg31.27
Envelope Rg envelope_rg26.77
Shape Rg shape_rg26.64
Total Rg total_rg27.19
Total atoms total_atoms2899
Residues n_residues363
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 dmax85.8
Rg (real space) rg_real27.14
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real2.6820e+07
I(0) uncertainty (real space) i0_real_error4.3280e+05
Rg (reciprocal space) rg_reciprocal27.06
I(0) (reciprocal space) i0_reciprocal26820000.0000
Solution quality estimate total_estimate0.8211
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.511
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4699000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.671; Smooth: 0.662

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6wv4A01
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 (2)

9. Files and Curves (10)