2rmk

Rac1/PRK1 Complex

Method: SOLUTION NMR Dmax: 78.8 Å Quality: GOOD

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

Ras-related C3 botulinum toxin substrate 1

Homo sapiens

UniProt P63000

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 1–192 Mutation:Q61L Serine/threonine-protein kinase N1 × 1 (Q16512) MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 0.225;Pressure ambient NMR sample composition:0.6mM [U-13C; U-15N; U-2H] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 13C; U-100% 15N] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 15N] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 13C; U-100% 15N] Rac1; 0.6mM PRK1 Rac1; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 15N] HR1b; 0.6mM PRK1 Rac1; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% 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.

74 other PDB entries and 102 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–192; UniProt 1–192

Serine/threonine-protein kinase N1

Homo sapiens

UniProt Q16512

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 122–199 Fragment:HR1b domain, REM 2, UNP residues 122-199 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 0.225;Pressure ambient NMR sample composition:0.6mM [U-13C; U-15N; U-2H] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 13C; U-100% 15N] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 15N] Rac1; 0.6mM PRK1 HR1b; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 13C; U-100% 15N] Rac1; 0.6mM PRK1 Rac1; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.6mM [U-100% 15N] HR1b; 0.6mM PRK1 Rac1; 0.7mM PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER; 90% H2O, 10% D2O | 90% H2O/10% 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.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PKN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–81; UniProt 122–199

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 2rmk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rmk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rmk
Deposition date deposition_date2007-10-25
Structure title titleRac1/PRK1 Complex
Keywords keywords;G protein, effector, ADP-ribosylation, Alternative splicing, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Polymorphism, Prenylation, ATP-binding, Cytoplasm, Kinase, Phosphorylation, Serine/threonine-protein kinase, Transferase, MEMBRANE PROTEIN-TRANSFERASE COMPLEX ;; MEMBRANE PROTEIN/TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.27
Radius of gyration Rg (electron density) rg_electron22.23
Forward intensity I(0) i08036210000.00
Molecular weight molecular_weight774880.0 kDa
Excluded volume excluded_volume975740 ų
Envelope volume envelope_volume73648 ų
Hydration-shell volume shell_volume25991 ų
Envelope diameter envelope_diameter86.2
Shell Rg shell_rg30.59
Envelope Rg envelope_rg25.58
Shape Rg shape_rg22.22
Total Rg total_rg22.33
Total atoms total_atoms110275
Residues n_residues6825
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 dmax78.8
Rg (real space) rg_real22.41
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real8.0360e+09
I(0) uncertainty (real space) i0_real_error1.1400e+08
Rg (reciprocal space) rg_reciprocal22.38
I(0) (reciprocal space) i0_reciprocal8036000000.0000
Solution quality estimate total_estimate0.8358
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.544
Kurtosis Kurtosis kurtosis-0.158
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1712000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.846; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2rmka_
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_idd2rmkb2
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.6 — HR1 repeat
Family Family familya.2.6.1 — HR1 repeat
Domain ID domain_idd2rmkb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2rmkA00
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_id2rmkB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily160 — HR1 repeat

8. Citations (1)

9. Files and Curves (10)