1ees

SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 61.3 Å Quality: GOOD

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

GTP-BINDING PROTEIN

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 A; UniProt 1–178 Fragment:AMINO ACIDS 1-178 P21-ACTIVATED KINASE × 1 (Q61036) SOLUTION NMR NMR measurement conditions:pH 5.5;298 K;Ionic strength (raw mmCIF value) 64 mM;Pressure ambient NMR sample composition:0.8 mM U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-15N Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N,13C PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM 70%-2H,U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-2H,15N Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 100% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N,13C PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 100% D2O Resolution not provided

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–178; UniProt 1–178

P21-ACTIVATED KINASE

Mus musculus

UniProt Q61036

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 63–108 Fragment:AMINO ACIDS 65-108 GTP-BINDING PROTEIN × 1 (P60953) SOLUTION NMR NMR measurement conditions:pH 5.5;298 K;Ionic strength (raw mmCIF value) 64 mM;Pressure ambient NMR sample composition:0.8 mM U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-15N Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N,13C PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM 70%-2H,U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-2H,15N Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 90% H2O/10% D2O NMR sample composition:0.8 mM U-15N,13C Cdc42Hs, 0.8 mM PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 100% D2O NMR sample composition:0.8 mM Cdc42Hs, 0.8 mM U-15N,13C PBD46; 25 mM NaCl, 5 mM Na2PO4, 5 mM MgCl2, 1 mM NaN3, pH 5.5 | 100% D2O Resolution not provided

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PAK3_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–46; UniProt 63–108

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 1ees

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ees
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ees
Deposition date deposition_date2000-02-02
Structure title titleSOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES
Keywords keywordsprotein-protein complex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.53
Radius of gyration Rg (electron density) rg_electron18.18
Forward intensity I(0) i03189680000.00
Molecular weight molecular_weight497170.0 kDa
Excluded volume excluded_volume628400 ų
Envelope volume envelope_volume70702 ų
Hydration-shell volume shell_volume26964 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg28.73
Envelope Rg envelope_rg21.29
Shape Rg shape_rg18.16
Total Rg total_rg18.39
Total atoms total_atoms70020
Residues n_residues4480
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 dmax61.3
Rg (real space) rg_real18.43
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.1900e+09
I(0) uncertainty (real space) i0_real_error3.7820e+07
Rg (reciprocal space) rg_reciprocal18.45
I(0) (reciprocal space) i0_reciprocal3190000000.0000
Solution quality estimate total_estimate0.8114
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha1427000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1eesa_
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
Domain ID domain_idd1eesb_
Class classj — Peptides
Fold Fold foldj.65 — Peptide derived from p-21 activated kinase
Superfamily Superfamily superfamilyj.65.1 — Peptide derived from p-21 activated kinase
Family Family familyj.65.1.1 — Peptide derived from p-21 activated kinase

CATH v4.4 (2 domains)

Domain ID domain_id1eesA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1eesB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology810 — SerineThreonine-protein kinase PAK-alpha; Chain A
Homologous superfamily homologous superfamily10 — CRIB domain

8. Citations (4)

9. Files and Curves (10)