8zjf

Cryo-EM structure of human integrin alpha-E beta-7

Method: ELECTRON MICROSCOPY Dmax: 152.4 Å Quality: REASONABLE

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

Integrin beta-7

Homo sapiens

UniProt P26010

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–798 Not recorded Integrin alpha-E × 1 (P38570) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–797; UniProt 2–798

Integrin alpha-E

Homo sapiens

UniProt P38570

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–1179 Not recorded Integrin beta-7 × 1 (P26010) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 ITAE_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–1178; UniProt 2–1179

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 8zjf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zjf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zjf
Deposition date deposition_date2024-05-14
Structure title titleCryo-EM structure of human integrin alpha-E beta-7
Keywords keywordsComplex, Cryo-EM, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.90
Radius of gyration Rg (electron density) rg_electron44.98
Forward intensity I(0) i0391351000.00
Molecular weight molecular_weight155690.0 kDa
Excluded volume excluded_volume192570 ų
Envelope volume envelope_volume290240 ų
Hydration-shell volume shell_volume57189 ų
Envelope diameter envelope_diameter160.5
Shell Rg shell_rg45.48
Envelope Rg envelope_rg44.74
Shape Rg shape_rg44.90
Total Rg total_rg45.26
Total atoms total_atoms10917
Residues n_residues1419
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 dmax152.4
Rg (real space) rg_real45.28
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real3.9140e+08
I(0) uncertainty (real space) i0_real_error7.1350e+06
Rg (reciprocal space) rg_reciprocal44.90
I(0) (reciprocal space) i0_reciprocal391200000.0000
Solution quality estimate total_estimate0.5823
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.577
Kurtosis Kurtosis kurtosis0.098
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24230000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 0.010; Positv: 1.000; Valcen: 0.897; Smooth: 0.154

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)