1h15

X-ray crystal structure of HLA-DRA1*0101/DRB5*0101 complexed with a peptide from Epstein Barr Virus DNA polymerase

Method: X-RAY DIFFRACTION Dmax: 85.1 Å Quality: EXCELLENT

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 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–207 Fragment:ALPHA CHAIN, RESIDUES 26-207 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN × 1 (Q30126) DNA POLYMERASE × 1 (P03198) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 26–207 Fragment:ALPHA CHAIN, RESIDUES 26-207 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN × 1 (Q30126) DNA POLYMERASE × 1 (P03198) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310

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 218 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HA2R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–182; UniProt 26–207 Author chain D; PDBConstruct 1–182; UniProt 26–207

HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN

HOMO SAPIENS

UniProt Q30126

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 30–219 Fragment:BETA CHAIN, RESIDUES 30-219 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) DNA POLYMERASE × 1 (P03198) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 30–219 Fragment:BETA CHAIN, RESIDUES 30-219 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) DNA POLYMERASE × 1 (P03198) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310

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 Q30126
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–190; UniProt 30–219 Author chain E; PDBConstruct 1–190; UniProt 30–219

DNA POLYMERASE

OrganismNot specified

UniProt P03198

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 628–641 Fragment:RESIDUES 628-641 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN × 1 (Q30126) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 628–641 Fragment:RESIDUES 628-641 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN × 1 (P01903) HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN × 1 (Q30126) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.5;14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. Resolution 3.10 Å R-free 0.310

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 DPOL_EBV
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–14; UniProt 628–641 Author chain F; PDBConstruct 1–14; UniProt 628–641

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 1h15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h15
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h15
Deposition date deposition_date2002-07-02
Structure title titleX-ray crystal structure of HLA-DRA1*0101/DRB5*0101 complexed with a peptide from Epstein Barr Virus DNA polymerase
Keywords keywords;IMMUNE SYSTEM/TRANSFERASE, COMPLEX (MHC-ANTIGEN), IMMUNE SYSTEM, MHC, HLA, CLASS II, DR2, DRB5, EBV, DNA POLYMERASE, DNA-DIRECTED DNA POLYMERASE, IMMUNE SYSTEM-TRANSFERASE complex ;; IMMUNE SYSTEM/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.07
Radius of gyration Rg (electron density) rg_electron27.86
Forward intensity I(0) i0134937000.00
Molecular weight molecular_weight90305.0 kDa
Excluded volume excluded_volume112400 ų
Envelope volume envelope_volume141360 ų
Hydration-shell volume shell_volume40989 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg36.34
Envelope Rg envelope_rg27.42
Shape Rg shape_rg27.85
Total Rg total_rg28.73
Total atoms total_atoms6390
Residues n_residues766
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 dmax85.1
Rg (real space) rg_real28.88
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.3490e+08
I(0) uncertainty (real space) i0_real_error1.5880e+06
Rg (reciprocal space) rg_reciprocal28.96
I(0) (reciprocal space) i0_reciprocal134900000.0000
Solution quality estimate total_estimate0.9106
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.050
Kurtosis Kurtosis kurtosis-0.596
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16560000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1h15a1
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_idd1h15a2
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_idd1h15b1
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_idd1h15b2
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_idd1h15d1
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_idd1h15d2
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_idd1h15e1
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_idd1h15e2
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 (8 domains)

Domain ID domain_id1h15A01
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_id1h15A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1h15B01
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_id1h15B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1h15D01
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_id1h15D02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1h15E01
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_id1h15E02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)