9t5v

Cryo-EM structure of alphaM/beta2:C3d-anti-CR3-Nb headpiece complex (HPO1 3D class reconstruction)

Method: ELECTRON MICROSCOPY Dmax: 199.6 Å Quality: REASONABLE

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 × 3 其他Polymer 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 17–773 Not recorded Integrin beta-2 × 1 (P05107) C3d-anti-CR3-Nb fusion ligand × 1 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 MN MANGANESE (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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 3.06 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 1–757; UniProt 17–773

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 × 3 其他Polymer 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 23–485 Not recorded Isoform 2 of Integrin alpha-M × 1 (P11215) C3d-anti-CR3-Nb fusion ligand × 1 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 MN MANGANESE (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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 3.06 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 1–463; UniProt 23–485

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 9t5v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t5v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t5v
Deposition date deposition_date2025-11-06
Structure title titleCryo-EM structure of alphaM/beta2:C3d-anti-CR3-Nb headpiece complex (HPO1 3D class reconstruction)
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_guinier57.91
Radius of gyration Rg (electron density) rg_electron59.02
Forward intensity I(0) i0516101000.00
Molecular weight molecular_weight184240.0 kDa
Excluded volume excluded_volume229150 ų
Envelope volume envelope_volume341360 ų
Hydration-shell volume shell_volume56448 ų
Envelope diameter envelope_diameter220.2
Shell Rg shell_rg47.25
Envelope Rg envelope_rg61.06
Shape Rg shape_rg58.95
Total Rg total_rg58.86
Total atoms total_atoms12928
Residues n_residues1632
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 dmax199.6
Rg (real space) rg_real58.78
Rg uncertainty (real space) rg_real_error1.98
I(0) (real space) i0_real5.1600e+08
I(0) uncertainty (real space) i0_real_error1.1910e+07
Rg (reciprocal space) rg_reciprocal57.15
I(0) (reciprocal space) i0_reciprocal514800000.0000
Solution quality estimate total_estimate0.5487
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.593
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0009
Highest regularization parameter α highest_alpha16610000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.701; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.511; Smooth: 0.514

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)