5ew3

Human Vascular Endothelial Growth Factor Receptor 2 (KDR) Kinase Domain in complex with AAL993

Method: X-RAY DIFFRACTION Dmax: 122.1 Å Quality: SUSPICIOUS

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

Vascular endothelial growth factor receptor 2

Homo sapiens

UniProt P35968

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 806–1171 Fragment:kinase domain, residues 806-1171 Mutation:E990V 5T2 2-(pyridin-4-ylmethylamino)-~{N}-[3-(trifluoromethyl)phenyl]benzamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;290 K;0.1M MES pH6.5, 8% w/v PEG 8000, 0.02M LITHIUM ACETATE Resolution 2.50 Å R-free 0.254
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 806–1171 Fragment:kinase domain, residues 806-1171 Mutation:E990V 5T2 2-(pyridin-4-ylmethylamino)-~{N}-[3-(trifluoromethyl)phenyl]benzamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;290 K;0.1M MES pH6.5, 8% w/v PEG 8000, 0.02M LITHIUM ACETATE Resolution 2.50 Å R-free 0.254

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.

53 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGFR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 806–1171 Author chain B; PDBConstruct 1–316; UniProt 806–1171

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 5ew3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ew3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ew3
Deposition date deposition_date2015-11-20
Structure title titleHuman Vascular Endothelial Growth Factor Receptor 2 (KDR) Kinase Domain in complex with AAL993
Keywords keywordskdr, kinase domain, ATP-binding site, VEGFR2 inhibitors, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.95
Radius of gyration Rg (electron density) rg_electron37.09
Forward intensity I(0) i056391300.00
Molecular weight molecular_weight62226.0 kDa
Excluded volume excluded_volume78664 ų
Envelope volume envelope_volume111960 ų
Hydration-shell volume shell_volume26148 ų
Envelope diameter envelope_diameter125.5
Shell Rg shell_rg41.85
Envelope Rg envelope_rg35.98
Shape Rg shape_rg37.08
Total Rg total_rg37.48
Total atoms total_atoms4377
Residues n_residues540
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 dmax122.1
Rg (real space) rg_real37.39
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real5.6390e+07
I(0) uncertainty (real space) i0_real_error1.0540e+06
Rg (reciprocal space) rg_reciprocal37.12
I(0) (reciprocal space) i0_reciprocal56380000.0000
Solution quality estimate total_estimate0.4989
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.796
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6608000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.543; Stabil: 1.000; Sysdev: 0.048; Positv: 1.000; Valcen: 0.285; Smooth: 0.424

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5ew3a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit
Domain ID domain_idd5ew3b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id5ew3A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5ew3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id5ew3B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5ew3B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (2)

9. Files and Curves (10)