4yc7

Crystal structure of human FMNL2 GBD-FH3 Domains bound to Cdc42-GppNHp

Method: X-RAY DIFFRACTION Dmax: 83.5 Å Quality: GOOD

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

Formin-like protein 2

Homo sapiens

UniProt Q96PY5

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 1–379 Fragment:UNP residues 1-379 Cell division control protein 42 homolog × 1 (P60953) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;20 mM Tris/HCl (pH 8.0), 14% (v/v) PEG 3350, 0.25 M magnesium acetate Resolution 2.50 Å R-free 0.253

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 FMNL2_HUMAN
Isoform Q96PY5-3
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 3–381; UniProt 1–379

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 A; UniProt 1–179 Fragment:UNP residues 1-179 Formin-like protein 2 × 1 (Q96PY5) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;20 mM Tris/HCl (pH 8.0), 14% (v/v) PEG 3350, 0.25 M magnesium acetate Resolution 2.50 Å R-free 0.253

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 P60953-1
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 3–181; UniProt 1–179

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 4yc7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yc7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yc7
Deposition date deposition_date2015-02-19
Structure title titleCrystal structure of human FMNL2 GBD-FH3 Domains bound to Cdc42-GppNHp
Keywords keywordssignaling protein, Armadillo repeat, Rho GTPase, cell cycle; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.22
Radius of gyration Rg (electron density) rg_electron24.20
Forward intensity I(0) i049150100.00
Molecular weight molecular_weight54663.0 kDa
Excluded volume excluded_volume68620 ų
Envelope volume envelope_volume83779 ų
Hydration-shell volume shell_volume28389 ų
Envelope diameter envelope_diameter85.6
Shell Rg shell_rg31.82
Envelope Rg envelope_rg24.34
Shape Rg shape_rg24.19
Total Rg total_rg25.11
Total atoms total_atoms3840
Residues n_residues470
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 dmax83.5
Rg (real space) rg_real25.12
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.9150e+07
I(0) uncertainty (real space) i0_real_error6.3500e+05
Rg (reciprocal space) rg_reciprocal25.15
I(0) (reciprocal space) i0_reciprocal49150000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.448
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11120000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4yc7a1
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_idd4yc7a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id4yc7A00
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)