9ecl

Structure of the human integrin beta2 transmembrane domain

Method: SOLUTION NMR Dmax: 75.6 Å Quality: REASONABLE

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 696–735 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;313.2 K;Ionic strength (raw mmCIF value) 0.025;Pressure 1 NMR sample composition:1.2 mM [U-100% 13C; U-100% 15N; U-80% 2H] alphaX peptide, 350 mM 1,2-dihexanoyl-sn-glycero-3-phosphoholine, 105 mM 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, 25 mM HEPES, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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 1
Chains and sequence ranges Author chain A; PDBConstruct 4–43; UniProt 696–735

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 9ecl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ecl
Deposition date deposition_date2024-11-14
Structure title titleStructure of the human integrin beta2 transmembrane domain
Keywords keywordsIntegrin, cell adhesion, receptor; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier20.30
Radius of gyration Rg (electron density) rg_electron19.26
Forward intensity I(0) i091879300.00
Molecular weight molecular_weight92932.0 kDa
Excluded volume excluded_volume121860 ų
Envelope volume envelope_volume26527 ų
Hydration-shell volume shell_volume9958 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg29.45
Envelope Rg envelope_rg26.43
Shape Rg shape_rg19.30
Total Rg total_rg19.50
Total atoms total_atoms13755
Residues n_residues903
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 dmax75.6
Rg (real space) rg_real20.94
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real9.1880e+07
I(0) uncertainty (real space) i0_real_error1.6330e+06
Rg (reciprocal space) rg_reciprocal20.83
I(0) (reciprocal space) i0_reciprocal91870000.0000
Solution quality estimate total_estimate0.5391
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks6
Primary peak position r_peak_primary4.3
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.750
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8659.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.004; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)