1ao7

COMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL PEPTIDE (TAX), AND HLA-A 0201

Method: X-RAY DIFFRACTION Dmax: 130.7 Å Quality: GOOD

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

HLA-A 0201

Homo sapiens

UniProt P01892

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 25–299 Fragment:EXTRACELLULAR DOMAINS ALPHA 1, ALPHA 2, ALPHA 3 BETA-2 MICROGLOBULIN × 1 (P61769) TAX PEPTIDE × 1 (P14079) T CELL RECEPTOR ALPHA × 1 T CELL RECEPTOR BETA × 1 EMC ETHYL MERCURY ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 25–299 Fragment:EXTRACELLULAR DOMAINS ALPHA 1, ALPHA 2, ALPHA 3 BETA-2 MICROGLOBULIN × 2 (P61769) TAX PEPTIDE × 2 (P14079) T CELL RECEPTOR ALPHA × 2 T CELL RECEPTOR BETA × 2 EMC ETHYL MERCURY ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320

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.

271 other PDB entries and 464 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1A02_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–275; UniProt 25–299

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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–119 Mutation:Y67C, K91C HLA-A 0201 × 1 (P01892) TAX PEPTIDE × 1 (P14079) T CELL RECEPTOR ALPHA × 1 T CELL RECEPTOR BETA × 1 EMC ETHYL MERCURY ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 21–119 Mutation:Y67C, K91C HLA-A 0201 × 2 (P01892) TAX PEPTIDE × 2 (P14079) T CELL RECEPTOR ALPHA × 2 T CELL RECEPTOR BETA × 2 EMC ETHYL MERCURY ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320

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 1997 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 2–100; UniProt 21–119

TAX PEPTIDE

Human T-lymphotropic virus 1

UniProt P14079

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 16–24 Fragment:RESIDUES 11 - 19 FROM TAX PROTEIN OF HUMAN T LYMPHOTROPIC VIRUS TYPE 1 HLA-A 0201 × 1 (P01892) BETA-2 MICROGLOBULIN × 1 (P61769) T CELL RECEPTOR ALPHA × 1 T CELL RECEPTOR BETA × 1 EMC ETHYL MERCURY ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 16–24 Fragment:RESIDUES 11 - 19 FROM TAX PROTEIN OF HUMAN T LYMPHOTROPIC VIRUS TYPE 1 HLA-A 0201 × 2 (P01892) BETA-2 MICROGLOBULIN × 2 (P61769) T CELL RECEPTOR ALPHA × 2 T CELL RECEPTOR BETA × 2 EMC ETHYL MERCURY ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZED FROM 10% PEG 8000, 100 MM MGACETATE, 50 MM NACACODYLATE, PH 6.5 Resolution 2.60 Å R-free 0.320

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAT_HTL1C
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 16–24

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 1ao7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ao7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ao7
Deposition date deposition_date1997-07-21
Structure title titleCOMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL PEPTIDE (TAX), AND HLA-A 0201
Keywords keywordsCLASS I MHC, T-CELL RECEPTOR, VIRAL PEPTIDE, COMPLEX (MHC-VIRAL PEPTIDE-RECEPTOR, COMPLEX (MHC-VIRAL PEPTIDE-RECEPTOR) COMPLEX; COMPLEX (MHC/VIRAL PEPTIDE/RECEPTOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.71
Radius of gyration Rg (electron density) rg_electron34.98
Forward intensity I(0) i0109429000.00
Molecular weight molecular_weight80774.0 kDa
Excluded volume excluded_volume99606 ų
Envelope volume envelope_volume133770 ų
Hydration-shell volume shell_volume34936 ų
Envelope diameter envelope_diameter138.2
Shell Rg shell_rg37.31
Envelope Rg envelope_rg35.90
Shape Rg shape_rg34.96
Total Rg total_rg35.22
Total atoms total_atoms5674
Residues n_residues707
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 dmax130.7
Rg (real space) rg_real35.19
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real1.0940e+08
I(0) uncertainty (real space) i0_real_error1.9250e+06
Rg (reciprocal space) rg_reciprocal34.89
I(0) (reciprocal space) i0_reciprocal109400000.0000
Solution quality estimate total_estimate0.7712
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.732
Kurtosis Kurtosis kurtosis0.139
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12090000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.498; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.637; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1ao7a1
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_idd1ao7a2
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_idd1ao7b2
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_idd1ao7b3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1ao7d_
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_idd1ao7e1
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_idd1ao7e2
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)

CATH v4.4 (6 domains)

Domain ID domain_id1ao7A01
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_id1ao7A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1ao7B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1ao7D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1ao7E01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1ao7E02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)