4ah2

HLA-DR1 with covalently linked CLIP106-120 in canonical orientation

Method: X-RAY DIFFRACTION Dmax: 83.7 Å Quality: GOOD

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

HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN

HOMO SAPIENS

UniProt P01903

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–217 Fragment:EXTRACELLULAR DOMAIN, RESIDUES 26-217 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN\,DRB1-1 BETA CHAIN × 1 (P04233,P04229) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;0.2 M LICL, 20% (W/V) PEG6000, 0.1 M HEPES, PH 7.0 Resolution 2.36 Å R-free 0.240

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.

139 other PDB entries and 219 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–193; UniProt 26–217

HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN\,DRB1-1 BETA CHAIN

HOMO SAPIENS

UniProt P04229

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 30–227 Fragment:EXTRACELLULAR DOMAIN, RESIDUES 106-120,30-227 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;0.2 M LICL, 20% (W/V) PEG6000, 0.1 M HEPES, PH 7.0 Resolution 2.36 Å R-free 0.240

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.

48 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2B11_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 32–229; UniProt 30–227

HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN\,DRB1-1 BETA CHAIN

HOMO SAPIENS

UniProt P04233

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 106–120 Fragment:EXTRACELLULAR DOMAIN, RESIDUES 106-120,30-227 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;0.2 M LICL, 20% (W/V) PEG6000, 0.1 M HEPES, PH 7.0 Resolution 2.36 Å R-free 0.240

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.

17 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HG2A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–16; UniProt 106–120

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 4ah2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ah2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ah2
Deposition date deposition_date2012-02-03
Structure title titleHLA-DR1 with covalently linked CLIP106-120 in canonical orientation
Keywords keywordsMHC II, IMMUNE SYSTEM, SELF ANTIGEN, INVARIANT CHAIN, CLIP; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.37
Radius of gyration Rg (electron density) rg_electron23.45
Forward intensity I(0) i032073300.00
Molecular weight molecular_weight43665.0 kDa
Excluded volume excluded_volume54618 ų
Envelope volume envelope_volume65659 ų
Hydration-shell volume shell_volume23709 ų
Envelope diameter envelope_diameter88.1
Shell Rg shell_rg30.02
Envelope Rg envelope_rg23.77
Shape Rg shape_rg23.42
Total Rg total_rg24.32
Total atoms total_atoms3081
Residues n_residues375
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 dmax83.7
Rg (real space) rg_real24.38
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.2070e+07
I(0) uncertainty (real space) i0_real_error4.6980e+05
Rg (reciprocal space) rg_reciprocal24.38
I(0) (reciprocal space) i0_reciprocal32070000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8567000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4ah2a1
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.19.1.0 — automated matches
Domain ID domain_idd4ah2a2
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

CATH v4.4 (4 domains)

Domain ID domain_id4ah2A01
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_id4ah2A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4ah2B01
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_id4ah2B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)