9k9n

Cryo-EM structure of MjHKU4r-CoV-1 receptor-binding domain complexed with human CD26

Method: ELECTRON MICROSCOPY Dmax: 146.5 Å Quality: GOOD

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

Dipeptidyl peptidase 4 soluble form

Homo sapiens

UniProt P27487

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 6 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 39–766 Chain B; UniProt 39–766 Not recorded Spike protein S1 × 1 (A0AAE8ZFM2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.61 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.

113 other PDB entries and 169 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 33–760; UniProt 39–766 Author chain B; PDBConstruct 33–760; UniProt 39–766

Spike protein S1

Tylonycteris bat coronavirus HKU4

UniProt A0AAE8ZFM2

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 6 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 389–595 Not recorded Dipeptidyl peptidase 4 soluble form × 2 (P27487) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.61 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.

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

View Construct and Data Evidence
UniProt name A0AAE8ZFM2_9BETC
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 19–225; UniProt 389–595

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 9k9n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9k9n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9k9n
Deposition date deposition_date2024-10-27
最后修订 last_revision2025-09-03
Structure title titleCryo-EM structure of MjHKU4r-CoV-1 receptor-binding domain complexed with human CD26
Keywords keywordsComplex, VIRAL PROTEIN/HYDROLASE, VIRAL PROTEIN-HYDROLASE complex; VIRAL PROTEIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.10
Radius of gyration Rg (electron density) rg_electron43.81
Forward intensity I(0) i0558748000.00
Molecular weight molecular_weight196100.0 kDa
Excluded volume excluded_volume245410 ų
Envelope volume envelope_volume354020 ų
Hydration-shell volume shell_volume67016 ų
Envelope diameter envelope_diameter148.4
Shell Rg shell_rg49.26
Envelope Rg envelope_rg43.07
Shape Rg shape_rg43.73
Total Rg total_rg44.32
Total atoms total_atoms13840
Residues n_residues1657
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 dmax146.5
Rg (real space) rg_real44.11
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real5.5870e+08
I(0) uncertainty (real space) i0_real_error1.0610e+07
Rg (reciprocal space) rg_reciprocal44.10
I(0) (reciprocal space) i0_reciprocal558700000.0000
Solution quality estimate total_estimate0.8807
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.8
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.571
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71290000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)