4ydh

The structure of human FMNL1 N-terminal domains bound to Cdc42

Method: X-RAY DIFFRACTION Dmax: 150.4 Å Quality: REASONABLE

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

Formin-like protein 1

Homo sapiens

UniProt O95466

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–458 Chain C; UniProt 1–458 Not recorded Cell division control protein 42 homolog × 2 (P60953) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;17% (v/v) PEG 3350, 0.16 M tri-ammonium citrate Resolution 3.80 Å R-free 0.281

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 FMNL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–433; UniProt 1–458 Author chain C; PDBConstruct 3–433; UniProt 1–458

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–179 Chain D; UniProt 1–179 Not recorded Formin-like protein 1 × 2 (O95466) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;17% (v/v) PEG 3350, 0.16 M tri-ammonium citrate Resolution 3.80 Å R-free 0.281

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 B; PDBConstruct 3–181; UniProt 1–179 Author chain D; 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 4ydh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ydh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4ydh
Deposition date deposition_date2015-02-22
Structure title titleThe structure of human FMNL1 N-terminal domains bound to Cdc42
Keywords keywordsactin cytoskeleton, GTPase, formin, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.39
Radius of gyration Rg (electron density) rg_electron43.74
Forward intensity I(0) i0180868000.00
Molecular weight molecular_weight107550.0 kDa
Excluded volume excluded_volume133400 ų
Envelope volume envelope_volume192230 ų
Hydration-shell volume shell_volume40059 ų
Envelope diameter envelope_diameter159.8
Shell Rg shell_rg43.10
Envelope Rg envelope_rg43.44
Shape Rg shape_rg43.73
Total Rg total_rg43.73
Total atoms total_atoms7564
Residues n_residues1014
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 dmax150.4
Rg (real space) rg_real43.81
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real1.8090e+08
I(0) uncertainty (real space) i0_real_error3.5980e+06
Rg (reciprocal space) rg_reciprocal43.40
I(0) (reciprocal space) i0_reciprocal180800000.0000
Solution quality estimate total_estimate0.5684
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.456
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17580000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.669; Stabil: 1.000; Sysdev: 0.032; Positv: 1.000; Valcen: 0.570; Smooth: 0.711

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4ydhB00
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_id4ydhD00
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)