2xfx

cattle MHC class I N01301 presenting an 11mer from Theileria parva

Method: X-RAY DIFFRACTION Dmax: 75.8 Å Quality: EXCELLENT

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

MHC CLASS 1

BOS TAURUS

UniProt Q30291

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 22–297 Fragment:RESIDUES 22-297 BETA-2-MICROGLOBULIN × 1 (P01888) UNCHARACTERIZED PROTEIN × 1 (Q4MYJ2) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% PEG 8000, 50MM POTASSIUM PHOSPHATE, PH 7.0 Resolution 1.90 Å R-free 0.238

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 Q30291_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 22–297

BETA-2-MICROGLOBULIN

BOS TAURUS

UniProt P01888

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 20–118 Not recorded MHC CLASS 1 × 1 (Q30291) UNCHARACTERIZED PROTEIN × 1 (Q4MYJ2) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% PEG 8000, 50MM POTASSIUM PHOSPHATE, PH 7.0 Resolution 1.90 Å R-free 0.238

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 20–118

UNCHARACTERIZED PROTEIN

OrganismNot specified

UniProt Q4MYJ2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 214–224 Fragment:214-224 MHC CLASS 1 × 1 (Q30291) BETA-2-MICROGLOBULIN × 1 (P01888) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% PEG 8000, 50MM POTASSIUM PHOSPHATE, PH 7.0 Resolution 1.90 Å R-free 0.238

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 Q4MYJ2_THEPA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–11; UniProt 214–224

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 2xfx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2xfx
Deposition date deposition_date2010-05-28
Structure title titlecattle MHC class I N01301 presenting an 11mer from Theileria parva
Keywords keywordsIMMUNE SYSTEM, MAJOR HISTOCOMPATIBILITY, EAST COAST FEVER, THEILERIOSIS; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.24
Radius of gyration Rg (electron density) rg_electron23.06
Forward intensity I(0) i037041500.00
Molecular weight molecular_weight45181.0 kDa
Excluded volume excluded_volume55747 ų
Envelope volume envelope_volume69005 ų
Hydration-shell volume shell_volume24979 ų
Envelope diameter envelope_diameter78.7
Shell Rg shell_rg29.97
Envelope Rg envelope_rg23.23
Shape Rg shape_rg23.02
Total Rg total_rg23.95
Total atoms total_atoms3192
Residues n_residues387
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 dmax75.8
Rg (real space) rg_real24.17
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.7040e+07
I(0) uncertainty (real space) i0_real_error5.0210e+05
Rg (reciprocal space) rg_reciprocal24.19
I(0) (reciprocal space) i0_reciprocal37040000.0000
Solution quality estimate total_estimate0.9094
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8346000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2xfxa1
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_idd2xfxa2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd2xfxa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2xfxb_
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 (3 domains)

Domain ID domain_id2xfxA01
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_id2xfxA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2xfxB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)