1ufu

Crystal structure of ligand binding domain of immunoglobulin-like transcript 2 (ILT2; LIR-1)

Method: X-RAY DIFFRACTION Dmax: 66.3 Å Quality: GOOD

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

Immunoglobulin-like transcript 2

Homo sapiens

UniProt Q8NHL6

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 25–221 Fragment:Ligand binding domain (domain1 and 2) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;1.6M Sodium Formate, 0.08M Na-acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.00 Å R-free 0.300

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIRB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–197; UniProt 25–221

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 1ufu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ufu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ufu
Deposition date deposition_date2003-06-10
Structure title titleCrystal structure of ligand binding domain of immunoglobulin-like transcript 2 (ILT2; LIR-1)
Keywords keywordsImmunoglobulin-like folds, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.51
Radius of gyration Rg (electron density) rg_electron18.75
Forward intensity I(0) i06694900.00
Molecular weight molecular_weight19198.0 kDa
Excluded volume excluded_volume24089 ų
Envelope volume envelope_volume28601 ų
Hydration-shell volume shell_volume13597 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg23.59
Envelope Rg envelope_rg19.06
Shape Rg shape_rg18.72
Total Rg total_rg19.61
Total atoms total_atoms1355
Residues n_residues171
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 dmax66.3
Rg (real space) rg_real19.61
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real6.6950e+06
I(0) uncertainty (real space) i0_real_error9.0330e+04
Rg (reciprocal space) rg_reciprocal19.59
I(0) (reciprocal space) i0_reciprocal6695000.0000
Solution quality estimate total_estimate0.8524
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1885000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.764; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ufua1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd1ufua2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains

CATH v4.4 (2 domains)

Domain ID domain_id1ufuA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1ufuA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)