9p95

CryoEM structure of integrin alpha4beta7 bound to MAdCAM-1

Method: ELECTRON MICROSCOPY Dmax: 146.5 Å Quality: GOOD

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

Integrin alpha-4

Homo sapiens

UniProt P13612

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 4 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–970 Not recorded Integrin beta-7 × 1 (P26010) Mucosal addressin cell adhesion molecule 1 × 1 (Q13477) ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3 MN MANGANESE (II) ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;0.05% CHAPS added immediately before vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITA4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–970; UniProt 1–970

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 × 3 其他Polymer 4 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–723 Not recorded Integrin alpha-4 × 1 (P13612) Mucosal addressin cell adhesion molecule 1 × 1 (Q13477) ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3 MN MANGANESE (II) ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;0.05% CHAPS added immediately before vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–723; UniProt 1–723

Mucosal addressin cell adhesion molecule 1

Homo sapiens

UniProt Q13477

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 4 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–317 Not recorded Integrin alpha-4 × 1 (P13612) Integrin beta-7 × 1 (P26010) ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3 MN MANGANESE (II) ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;0.05% CHAPS added immediately before vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

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

View Construct and Data Evidence
UniProt name MADCA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–317; UniProt 1–317

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 9p95

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p95
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p95
Deposition date deposition_date2025-06-24
最后修订 last_revision2025-09-24
Structure title titleCryoEM structure of integrin alpha4beta7 bound to MAdCAM-1
Keywords keywordsa4b7, gut adhesion, lymphocyte homing, membrane receptor, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.67
Radius of gyration Rg (electron density) rg_electron40.80
Forward intensity I(0) i0271043000.00
Molecular weight molecular_weight130260.0 kDa
Excluded volume excluded_volume161790 ų
Envelope volume envelope_volume226360 ų
Hydration-shell volume shell_volume49784 ų
Envelope diameter envelope_diameter156.9
Shell Rg shell_rg41.89
Envelope Rg envelope_rg41.66
Shape Rg shape_rg40.79
Total Rg total_rg40.91
Total atoms total_atoms18066
Residues n_residues1162
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_real40.89
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real2.7100e+08
I(0) uncertainty (real space) i0_real_error5.1930e+06
Rg (reciprocal space) rg_reciprocal40.68
I(0) (reciprocal space) i0_reciprocal271000000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis-0.256
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33700000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.722; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.695; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)