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1wfs

Solution Structure of Glia Maturation Factor-gamma from Mus Musculus

Method: SOLUTION NMR Dmax: 57.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glia maturation factor gamma

Mus musculus

UniProt Q9ERL7

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 2–139 Fragment：COFILIN-ADF-domain No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition：1.21mM cofilin U-15N,13C; 20mM phosphate buffer Na; 100mM NaCl; 0.02% NaN3; 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.

Other PDB Difference from Current Entry 1WFS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1VKK Crystal structure of Glia maturation factor-gamma (GMFG) from Mus musculus at 1.50 A resolution Deposited 2004-05-27 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–142（142 aa）
Not recorded PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION,SITTING DROP,NANODROP；pH 8.5；277 K；30% PEG-4000, 0.1M Tris hydrochloride pH 8.5,0.2M lithium sulfate monohydrate, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K
Resolution 1.35 Å R-free 0.194
4JD2 Crystal structure of Bos taurus Arp2/3 complex binding with Mus musculus GMF Deposited 2013-02-22 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain H 1–142（142 aa）
Not recorded CA CALCIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PG4 TETRAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.08 Å R-free 0.248

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GMFG_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–145； UniProt 2–139

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 1wfs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1wfs
Deposition date deposition_date2004-05-26
Structure title titleSolution Structure of Glia Maturation Factor-gamma from Mus Musculus
Keywords keywordsACTIN BINDING PROTEIN, CYTOSKELETON, STRUCTURAL GENOMICS, RIKEN Structural Genomics/Proteomics Initiative, RSGI, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.44 Å
Radius of gyration Rg (electron density) rg_electron15.65 Å
Forward intensity I(0) i01649000000.00
Molecular weight molecular_weight342770.0 kDa
Excluded volume excluded_volume428260 ų
Envelope volume envelope_volume42151 ų
Hydration-shell volume shell_volume18994 ų
Envelope diameter envelope_diameter66.6 Å
Shell Rg shell_rg25.11 Å
Envelope Rg envelope_rg19.30 Å
Shape Rg shape_rg15.62 Å
Total Rg total_rg15.89 Å
Total atoms total_atoms48060
Residues n_residues3020
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax57.8 Å
Rg (real space) rg_real16.42 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real1.6490e+09
I(0) uncertainty (real space) i0_real_error2.3130e+07
Rg (reciprocal space) rg_reciprocal16.42 Å
I(0) (reciprocal space) i0_reciprocal1649000000.0000
Solution quality estimate total_estimate0.7612
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.5 Å
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis0.006
Angular range angular_range— – 0.4850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha912200.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.636; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1wfsa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.109 — Gelsolin-like
Superfamily Superfamily superfamilyd.109.1 — Actin depolymerizing proteins
Family Family familyd.109.1.2 — Cofilin-like
Domain ID domain_idd1wfsa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1wfsa3
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_id1wfsA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
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8. Citations (1)

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9. Files and Curves (10)