2e7l

Structure of a high-affinity mutant of the 2C TCR in complex with Ld/QL9

Method: X-RAY DIFFRACTION Dmax: 112.8 Å Quality: GOOD

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

Cytotoxic Tcell receptor

Mus musculus

UniProt A2NTU7

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 21–132 Fragment:UNP RESIDUES 21-132 Beta-chain × 1 (A2NTY6) H-2 class I histocompatibility antigen, L-D alpha chain × 1 (P01897) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 21–132 Fragment:UNP RESIDUES 21-132 Beta-chain × 1 (A2NTY6) H-2 class I histocompatibility antigen, L-D alpha chain × 1 (P01897) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A2NTU7_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–112; UniProt 21–132 Author chain B; PDBConstruct 1–112; UniProt 21–132

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 30–144 Fragment:UNP RESIDUES 30-144 Cytotoxic Tcell receptor × 1 (A2NTU7) H-2 class I histocompatibility antigen, L-D alpha chain × 1 (P01897) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 30–144 Fragment:UNP RESIDUES 30-144 Cytotoxic Tcell receptor × 1 (A2NTU7) H-2 class I histocompatibility antigen, L-D alpha chain × 1 (P01897) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246

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 25 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 C; PDBConstruct 1–110; UniProt 30–144 Author chain D; PDBConstruct 1–110; UniProt 30–144

H-2 class I histocompatibility antigen, L-D alpha chain

Mus musculus

UniProt P01897

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 25–205 Fragment:alpha 1,2 domains (UNP RESIDUES 25-205) Cytotoxic Tcell receptor × 1 (A2NTU7) Beta-chain × 1 (A2NTY6) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 25–205 Fragment:alpha 1,2 domains (UNP RESIDUES 25-205) Cytotoxic Tcell receptor × 1 (A2NTU7) Beta-chain × 1 (A2NTY6) Peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;298 K;0.2M ammonium phosphate, 20% PEG 3350, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.50 Å R-free 0.246

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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA1L_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–181; UniProt 25–205 Author chain F; PDBConstruct 1–181; UniProt 25–205

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 2e7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2e7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2e7l
Deposition date deposition_date2007-01-11
Structure title titleStructure of a high-affinity mutant of the 2C TCR in complex with Ld/QL9
Keywords keywordsTCR, MHC, 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_guinier31.89
Radius of gyration Rg (electron density) rg_electron31.22
Forward intensity I(0) i0140964000.00
Molecular weight molecular_weight92090.0 kDa
Excluded volume excluded_volume113980 ų
Envelope volume envelope_volume141340 ų
Hydration-shell volume shell_volume37654 ų
Envelope diameter envelope_diameter121.3
Shell Rg shell_rg38.17
Envelope Rg envelope_rg31.10
Shape Rg shape_rg31.17
Total Rg total_rg31.95
Total atoms total_atoms6509
Residues n_residues814
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 dmax112.8
Rg (real space) rg_real31.88
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.4100e+08
I(0) uncertainty (real space) i0_real_error2.2310e+06
Rg (reciprocal space) rg_reciprocal31.89
I(0) (reciprocal space) i0_reciprocal141000000.0000
Solution quality estimate total_estimate0.8716
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.1
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.416
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22540000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2e7la_
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_idd2e7lb_
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_idd2e7lc_
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_idd2e7ld_
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)

CATH v4.4 (6 domains)

Domain ID domain_id2e7lA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2e7lB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2e7lC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2e7lD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2e7lE00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id2e7lF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like

8. Citations (1)

9. Files and Curves (10)