1m1l

Human Suppressor of Fused (N-terminal domain)

Method: X-RAY DIFFRACTION Dmax: 101.4 Å Quality: EXCELLENT

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

Suppressor of Fused

Homo sapiens

UniProt Q9UMX1

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 27–262 Chain B; UniProt 27–262 Chain C; UniProt 27–262 Chain D; UniProt 27–262 Fragment:N-terminal domain (Residues 27-262) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;279 K;1 M LiCl, 0.1 M NaCitrate pH 5.0- 6.0, 10% w/v PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 2.65 Å R-free 0.256

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.

9 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUFU_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–236; UniProt 27–262 Author chain B; PDBConstruct 1–236; UniProt 27–262 Author chain C; PDBConstruct 1–236; UniProt 27–262 Author chain D; PDBConstruct 1–236; UniProt 27–262

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 1m1l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m1l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m1l
Deposition date deposition_date2002-06-19
Structure title titleHuman Suppressor of Fused (N-terminal domain)
Keywords keywordsGene regulation, Hedgehog signaling, signal transduction, fused, 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_guinier32.70
Radius of gyration Rg (electron density) rg_electron31.60
Forward intensity I(0) i0179311000.00
Molecular weight molecular_weight105900.0 kDa
Excluded volume excluded_volume131810 ų
Envelope volume envelope_volume165360 ų
Hydration-shell volume shell_volume42886 ų
Envelope diameter envelope_diameter102.0
Shell Rg shell_rg39.24
Envelope Rg envelope_rg31.27
Shape Rg shape_rg31.61
Total Rg total_rg32.20
Total atoms total_atoms7486
Residues n_residues940
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 dmax101.4
Rg (real space) rg_real32.51
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.7930e+08
I(0) uncertainty (real space) i0_real_error2.6960e+06
Rg (reciprocal space) rg_reciprocal32.60
I(0) (reciprocal space) i0_reciprocal179300000.0000
Solution quality estimate total_estimate0.9085
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.2
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34320000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1m1la_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.260 — Suppressor of Fused, N-terminal domain
Superfamily Superfamily superfamilyd.260.1 — Suppressor of Fused, N-terminal domain
Family Family familyd.260.1.1 — Suppressor of Fused, N-terminal domain
Domain ID domain_idd1m1lb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.260 — Suppressor of Fused, N-terminal domain
Superfamily Superfamily superfamilyd.260.1 — Suppressor of Fused, N-terminal domain
Family Family familyd.260.1.1 — Suppressor of Fused, N-terminal domain
Domain ID domain_idd1m1lc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.260 — Suppressor of Fused, N-terminal domain
Superfamily Superfamily superfamilyd.260.1 — Suppressor of Fused, N-terminal domain
Family Family familyd.260.1.1 — Suppressor of Fused, N-terminal domain
Domain ID domain_idd1m1ld_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.260 — Suppressor of Fused, N-terminal domain
Superfamily Superfamily superfamilyd.260.1 — Suppressor of Fused, N-terminal domain
Family Family familyd.260.1.1 — Suppressor of Fused, N-terminal domain

8. Citations (1)

9. Files and Curves (10)