8glh

Crystal Structure of Human CD1b in Complex with Endogenous PC C40:5

Method: X-RAY DIFFRACTION Dmax: 76.7 Å Quality: REASONABLE

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

T-cell surface glycoprotein CD1b

Homo sapiens

UniProt P29016

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 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 20–296 Not recorded Beta-2-microglobulin × 1 (P61769) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 IOD IODIDE ION × 3 3IV (11E)-hexadec-11-enoic acid × 1 3IY [(2~{R})-1-dodecanoyloxy-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propan-2-yl] (8~{Z},11~{Z},14~{Z},24~{Z},27~{Z})-triaconta-8,11,14,24,27-pentaenoate × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;24% PEG3350, 0.2 M sodium iodide, 2% ethylene glycol Resolution 1.83 Å R-free 0.221

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.

27 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–277; UniProt 20–296

Beta-2-microglobulin

Homo sapiens

UniProt P61769

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 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded T-cell surface glycoprotein CD1b × 1 (P29016) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 IOD IODIDE ION × 3 3IV (11E)-hexadec-11-enoic acid × 1 3IY [(2~{R})-1-dodecanoyloxy-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propan-2-yl] (8~{Z},11~{Z},14~{Z},24~{Z},27~{Z})-triaconta-8,11,14,24,27-pentaenoate × 1 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;24% PEG3350, 0.2 M sodium iodide, 2% ethylene glycol Resolution 1.83 Å R-free 0.221

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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–101; UniProt 21–119

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 8glh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8glh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8glh
Deposition date deposition_date2023-03-22
Structure title titleCrystal Structure of Human CD1b in Complex with Endogenous PC C40:5
Keywords keywordsAntigen Presentation, Lipid, CD1b, phospholipid, 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_guinier24.99
Radius of gyration Rg (electron density) rg_electron23.79
Forward intensity I(0) i034655400.00
Molecular weight molecular_weight45990.0 kDa
Excluded volume excluded_volume57643 ų
Envelope volume envelope_volume70861 ų
Hydration-shell volume shell_volume24989 ų
Envelope diameter envelope_diameter78.9
Shell Rg shell_rg30.71
Envelope Rg envelope_rg23.91
Shape Rg shape_rg23.72
Total Rg total_rg24.83
Total atoms total_atoms3220
Residues n_residues380
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 dmax76.7
Rg (real space) rg_real24.93
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.4660e+07
I(0) uncertainty (real space) i0_real_error3.9760e+05
Rg (reciprocal space) rg_reciprocal24.95
I(0) (reciprocal space) i0_reciprocal34660000.0000
Solution quality estimate total_estimate0.7259
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4532000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 0.184; Positv: 1.000; Valcen: 0.998; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)