8tq4

Crystal structure of Fab M142 in complex with MHC-I (H2-Dd)

Method: X-RAY DIFFRACTION Dmax: 142.0 Å Quality: GOOD

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

H2 class I histocompatibility antigen D-d alpha chain (H2-Dd)

Mus musculus

UniProt P01900

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 26–298 Not recorded Beta-2-microglobulin × 1 (P01887) Fab M142 Heavy Chain × 1 Fab M142 Light Chain × 1 HV1: HIV-1 P18-I10 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;10% PEG4000, 0.2 M sodium acetate, 0.1 M sodium citrate, pH 5.5 Resolution 3.59 Å R-free 0.270
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 26–298 Not recorded Beta-2-microglobulin × 1 (P01887) Fab M142 Heavy Chain × 1 Fab M142 Light Chain × 1 HV1: HIV-1 P18-I10 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;10% PEG4000, 0.2 M sodium acetate, 0.1 M sodium citrate, pH 5.5 Resolution 3.59 Å R-free 0.270

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 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA12_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–273; UniProt 26–298 Author chain E; PDBConstruct 1–273; UniProt 26–298

Beta-2-microglobulin

Mus musculus

UniProt P01887

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–118 Not recorded H2 class I histocompatibility antigen D-d alpha chain (H2-Dd) × 1 (P01900) Fab M142 Heavy Chain × 1 Fab M142 Light Chain × 1 HV1: HIV-1 P18-I10 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;10% PEG4000, 0.2 M sodium acetate, 0.1 M sodium citrate, pH 5.5 Resolution 3.59 Å R-free 0.270
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 21–118 Not recorded H2 class I histocompatibility antigen D-d alpha chain (H2-Dd) × 1 (P01900) Fab M142 Heavy Chain × 1 Fab M142 Light Chain × 1 HV1: HIV-1 P18-I10 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;10% PEG4000, 0.2 M sodium acetate, 0.1 M sodium citrate, pH 5.5 Resolution 3.59 Å R-free 0.270

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.

290 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–98; UniProt 21–118 Author chain F; PDBConstruct 1–98; UniProt 21–118

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 8tq4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tq4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tq4
Deposition date deposition_date2023-08-06
最后修订 last_revision2025-02-05
Structure title titleCrystal structure of Fab M142 in complex with MHC-I (H2-Dd)
Keywords keywords;histocompatibility complex class I, MHC-I, immune response, immune system Fab, antibody, anti-MHC antibody, cancer tumor, 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_guinier42.62
Radius of gyration Rg (electron density) rg_electron42.50
Forward intensity I(0) i0501162000.00
Molecular weight molecular_weight179750.0 kDa
Excluded volume excluded_volume223000 ų
Envelope volume envelope_volume314420 ų
Hydration-shell volume shell_volume61662 ų
Envelope diameter envelope_diameter147.5
Shell Rg shell_rg47.31
Envelope Rg envelope_rg42.11
Shape Rg shape_rg42.46
Total Rg total_rg42.87
Total atoms total_atoms12671
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 dmax142.0
Rg (real space) rg_real42.63
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real5.0120e+08
I(0) uncertainty (real space) i0_real_error8.8060e+06
Rg (reciprocal space) rg_reciprocal42.62
I(0) (reciprocal space) i0_reciprocal501200000.0000
Solution quality estimate total_estimate0.8871
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.1
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44460000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)