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2kcx

Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.

Method: SOLUTION NMR Dmax: 55.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Follistatin-related protein 3

Homo sapiens

UniProt O95633

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 97–169 Fragment：Kazal-1 domain, residues 97-169 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.2；Pressure ambient NMR sample composition：0.6 mM [U-100% 13C; U-100% 15N] FSTL-3-1, 20 mM MES-2, 200 mM sodium chloride-3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.2 mM [U-100% 15N] FSTL-3-4, 20 mM MES-5, 200 mM sodium chloride-6, 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.

Other PDB Difference from Current Entry 2KCX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3B4V X-Ray structure of Activin in complex with FSTL3 Deposited 2007-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 27–263（237 aa）
Chain D 27–263（237 aa）
Not recorded EDO 1,2-ETHANEDIOL × 2 SO4 SULFATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 3350, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.48 Å R-free 0.279
3B4V X-Ray structure of Activin in complex with FSTL3 Deposited 2007-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain G 27–263（237 aa）
Chain H 27–263（237 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 3350, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.48 Å R-free 0.279
3SEK Crystal Structure of the Myostatin:Follistatin-like 3 Complex Deposited 2011-06-10 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 36–244（209 aa） Fragment：UNP Residues 36-244
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 7.5；293 K；potassium thiocyanate, PEG 3350, pH 7.5, hanging drop, temperature 293K
Resolution 2.40 Å R-free 0.270

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FSTL3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–74； UniProt 97–169

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 2kcx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2kcx
Deposition date deposition_date2008-12-30
Structure title titleSolution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Keywords keywords;Kazal-1, Follistatin, Chromosomal rearrangement, Glycoprotein, Nucleus, Proto-oncogene, Secreted, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, unknown function, NUCLEOTIDE-BINDING PROTEIN ;; structural genomics, unknown function
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.84 Å
Radius of gyration Rg (electron density) rg_electron14.94 Å
Forward intensity I(0) i0499512000.00
Molecular weight molecular_weight159400.0 kDa
Excluded volume excluded_volume188310 ų
Envelope volume envelope_volume24599 ų
Hydration-shell volume shell_volume13046 ų
Envelope diameter envelope_diameter60.5 Å
Shell Rg shell_rg21.81 Å
Envelope Rg envelope_rg17.33 Å
Shape Rg shape_rg14.91 Å
Total Rg total_rg15.16 Å
Total atoms total_atoms21320
Residues n_residues1480
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 dmax55.5 Å
Rg (real space) rg_real15.02 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real4.9950e+08
I(0) uncertainty (real space) i0_real_error5.9500e+06
Rg (reciprocal space) rg_reciprocal15.01 Å
I(0) (reciprocal space) i0_reciprocal499500000.0000
Solution quality estimate total_estimate0.7053
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.3 Å
Skewness Skewness skewness0.539
Kurtosis Kurtosis kurtosis-0.285
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha214100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.623; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.298; 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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2kcxA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily30 —
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8. Citations (1)

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9. Files and Curves (10)