9t5w

Cryo-EM structure of mutant R61H alphaM/beta2 headpiece complex

Method: ELECTRON MICROSCOPY Dmax: 164.1 Å Quality: GOOD

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

Isoform 2 of Integrin alpha-M

Homo sapiens

UniProt P11215

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 5 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 17–770 Not recorded Integrin beta-2 × 1 (P05107) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 MN MANGANESE (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;0.02 % w/v CHAPS added to sample just before vitrification Resolution 2.74 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.

30 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITAM_HUMAN
Isoform P11215-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–754; UniProt 17–770

Integrin beta-2

Homo sapiens

UniProt P05107

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 5 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 23–482 Not recorded Isoform 2 of Integrin alpha-M × 1 (P11215) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 MN MANGANESE (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;0.02 % w/v CHAPS added to sample just before vitrification Resolution 2.74 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.

24 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–460; UniProt 23–482

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 9t5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t5w
Deposition date deposition_date2025-11-06
Structure title titleCryo-EM structure of mutant R61H alphaM/beta2 headpiece complex
Keywords keywordsphagocytosis, integrin, opsonisation, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.61
Radius of gyration Rg (electron density) rg_electron48.02
Forward intensity I(0) i0300139000.00
Molecular weight molecular_weight137540.0 kDa
Excluded volume excluded_volume170680 ų
Envelope volume envelope_volume247110 ų
Hydration-shell volume shell_volume48833 ų
Envelope diameter envelope_diameter175.0
Shell Rg shell_rg43.23
Envelope Rg envelope_rg49.90
Shape Rg shape_rg47.94
Total Rg total_rg48.06
Total atoms total_atoms19071
Residues n_residues1210
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 dmax164.1
Rg (real space) rg_real48.32
Rg uncertainty (real space) rg_real_error2.08
I(0) (real space) i0_real3.0010e+08
I(0) uncertainty (real space) i0_real_error6.6960e+06
Rg (reciprocal space) rg_reciprocal47.61
I(0) (reciprocal space) i0_reciprocal299900000.0000
Solution quality estimate total_estimate0.7860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19170000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.658; Smooth: 0.404

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)