2pxy

Crystal structures of immune receptor complexes

Method: X-RAY DIFFRACTION Dmax: 107.8 Å Quality: GOOD

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

T cell receptor alpha chain

Mus musculus

UniProt Q5R1F5

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 21–112 Not recorded T cell receptor beta chain × 1 (A2NTY6) H-2 class II histocompatibility antigen, A-U alpha chain × 1 (P14438) H-2 class II histocompatibility antigen, A-U beta chain × 1 (P06344) Myelin basic protein (MBP)-peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;0.2M Potassium sodium tartrate tetrahydrate, 0.1M succinic acid (pH7.0), 16% polyethylene glycol 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.23 Å R-free 0.253

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5R1F5_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–94; UniProt 21–112

T cell receptor beta chain

Mus musculus

UniProt A2NTY6

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 32–144 Mutation:G17E,H47Y,I75T,L78S T cell receptor alpha chain × 1 (Q5R1F5) H-2 class II histocompatibility antigen, A-U alpha chain × 1 (P14438) H-2 class II histocompatibility antigen, A-U beta chain × 1 (P06344) Myelin basic protein (MBP)-peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;0.2M Potassium sodium tartrate tetrahydrate, 0.1M succinic acid (pH7.0), 16% polyethylene glycol 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.23 Å R-free 0.253

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.

15 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A2NTY6_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–111; UniProt 32–144

H-2 class II histocompatibility antigen, A-U alpha chain

Mus musculus

UniProt P14438

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 C; UniProt 1–178 Fragment:extracellular alpha-1, extracellular alpha-2 T cell receptor alpha chain × 1 (Q5R1F5) T cell receptor beta chain × 1 (A2NTY6) H-2 class II histocompatibility antigen, A-U beta chain × 1 (P06344) Myelin basic protein (MBP)-peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;0.2M Potassium sodium tartrate tetrahydrate, 0.1M succinic acid (pH7.0), 16% polyethylene glycol 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.23 Å R-free 0.253

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA2U_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–183; UniProt 1–178

H-2 class II histocompatibility antigen, A-U beta chain

Mus musculus

UniProt P06344

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 D; UniProt 29–217 Fragment:extracellular beta-1, extracellular beta-2 T cell receptor alpha chain × 1 (Q5R1F5) T cell receptor beta chain × 1 (A2NTY6) H-2 class II histocompatibility antigen, A-U alpha chain × 1 (P14438) Myelin basic protein (MBP)-peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;0.2M Potassium sodium tartrate tetrahydrate, 0.1M succinic acid (pH7.0), 16% polyethylene glycol 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.23 Å R-free 0.253

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HB2U_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–189; UniProt 29–217

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 2pxy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pxy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pxy
Deposition date deposition_date2007-05-14
Structure title titleCrystal structures of immune receptor complexes
Keywords keywordscomplex, 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_guinier29.95
Radius of gyration Rg (electron density) rg_electron29.66
Forward intensity I(0) i079448400.00
Molecular weight molecular_weight69074.0 kDa
Excluded volume excluded_volume85732 ų
Envelope volume envelope_volume105880 ų
Hydration-shell volume shell_volume31577 ų
Envelope diameter envelope_diameter116.5
Shell Rg shell_rg34.64
Envelope Rg envelope_rg30.34
Shape Rg shape_rg29.59
Total Rg total_rg30.31
Total atoms total_atoms4883
Residues n_residues604
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 dmax107.8
Rg (real space) rg_real30.21
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real7.9450e+07
I(0) uncertainty (real space) i0_real_error1.3380e+06
Rg (reciprocal space) rg_reciprocal30.10
I(0) (reciprocal space) i0_reciprocal79440000.0000
Solution quality estimate total_estimate0.8291
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.622
Kurtosis Kurtosis kurtosis0.058
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11840000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.805; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd2pxya_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2pxyb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2pxyc1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd2pxyc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd2pxyc3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2pxyd1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd2pxyd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain

CATH v4.4 (6 domains)

Domain ID domain_id2pxyA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2pxyB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2pxyC01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology320 — Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1
Domain ID domain_id2pxyC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2pxyD01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology320 — Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1
Domain ID domain_id2pxyD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)