6n7h

Cryo-EM structure of the 2:1 hPtch1-Shhp complex

Method: ELECTRON MICROSCOPY Dmax: 153.2 Å Quality: GOOD

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

Protein patched homolog 1

Homo sapiens

UniProt Q13635

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1305 Chain B; UniProt 1–1305 Not recorded Sonic hedgehog protein × 1 (Q15465) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 CLR CHOLESTEROL × 5 ZN ZINC ION × 1 CA CALCIUM ION × 2 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–1326; UniProt 1–1305 Author chain B; PDBConstruct 22–1326; UniProt 1–1305

Sonic hedgehog protein

Homo sapiens

UniProt Q15465

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 24–197 Not recorded Protein patched homolog 1 × 2 (Q13635) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 CLR CHOLESTEROL × 5 ZN ZINC ION × 1 CA CALCIUM ION × 2 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

18 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SHH_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–174; UniProt 24–197

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 6n7h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n7h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n7h
Deposition date deposition_date2018-11-27
Structure title titleCryo-EM structure of the 2:1 hPtch1-Shhp complex
Keywords keywordsReceptor, RND family, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.04
Radius of gyration Rg (electron density) rg_electron48.45
Forward intensity I(0) i0758797000.00
Molecular weight molecular_weight244480.0 kDa
Excluded volume excluded_volume311820 ų
Envelope volume envelope_volume450440 ų
Hydration-shell volume shell_volume74153 ų
Envelope diameter envelope_diameter156.9
Shell Rg shell_rg56.65
Envelope Rg envelope_rg47.19
Shape Rg shape_rg48.43
Total Rg total_rg48.82
Total atoms total_atoms17242
Residues n_residues2153
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 dmax153.2
Rg (real space) rg_real48.83
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real7.5880e+08
I(0) uncertainty (real space) i0_real_error1.3670e+07
Rg (reciprocal space) rg_reciprocal49.04
I(0) (reciprocal space) i0_reciprocal759000000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.8
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.757
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102200000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.778

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6n7hC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1380 — Muramoyl-pentapeptide Carboxypeptidase; domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)