5upl

CDC42 binds PAK4 via an extended GTPase-effector inteface - 2 peptide: PAK4FL, CDC42 - UNREFINED

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: EXCELLENT

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

Serine/threonine-protein kinase PAK 4

Homo sapiens

UniProt O96013

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–426 Fragment:UNP residues 2-426 Mutation:S474SEP Non-standard monomer:Yes (specific site not provided by mmCIF) Cell division control protein 42 homolog × 1 (P60953) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;0.1M Tris-HCl pH 8.5, 50mM Na2SO4, 6% PEG6000 Resolution 3.00 Å R-free 0.310

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.

46 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAK4_HUMAN
Isoform O96013-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 29–453; UniProt 2–426

Cell division control protein 42 homolog

Homo sapiens

UniProt P60953

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–177 Fragment:UNP residues 1-177 Serine/threonine-protein kinase PAK 4 × 1 (O96013) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;0.1M Tris-HCl pH 8.5, 50mM Na2SO4, 6% PEG6000 Resolution 3.00 Å R-free 0.310

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.

45 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC42_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–177; UniProt 1–177

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 5upl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5upl
Deposition date deposition_date2017-02-03
Structure title titleCDC42 binds PAK4 via an extended GTPase-effector inteface - 2 peptide: PAK4FL, CDC42 - UNREFINED
Keywords keywordsTransferase, GTPase, Kinase, CRIB; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.43
Radius of gyration Rg (electron density) rg_electron25.54
Forward intensity I(0) i042544400.00
Molecular weight molecular_weight51757.0 kDa
Excluded volume excluded_volume65482 ų
Envelope volume envelope_volume81331 ų
Hydration-shell volume shell_volume27179 ų
Envelope diameter envelope_diameter88.3
Shell Rg shell_rg32.10
Envelope Rg envelope_rg25.47
Shape Rg shape_rg25.57
Total Rg total_rg26.22
Total atoms total_atoms3639
Residues n_residues466
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 dmax84.2
Rg (real space) rg_real26.44
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real4.2540e+07
I(0) uncertainty (real space) i0_real_error5.7600e+05
Rg (reciprocal space) rg_reciprocal26.44
I(0) (reciprocal space) i0_reciprocal42540000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10010000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5upla_
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.144.1.0 — automated matches
Domain ID domain_idd5uplb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (3 domains)

Domain ID domain_id5uplA01
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_id5uplA02
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_id5uplB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)