6eny

Structure of the human PLC editing module

Method: ELECTRON MICROSCOPY Dmax: 136.9 Å Quality: GOOD

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

Beta-2-microglobulin

OrganismNot specified

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 Other combination Heteromer Protein × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded Tapasin × 1 (O15533) Protein disulfide-isomerase A3 × 1 (P30101) HLA class I histocompatibility antigen, A-3 alpha chain × 1 (P04439) Calreticulin × 1 (P27797) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 21–119

Tapasin

OrganismNot specified

UniProt O15533

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 × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 21–448 Not recorded Beta-2-microglobulin × 1 (P61769) Protein disulfide-isomerase A3 × 1 (P30101) HLA class I histocompatibility antigen, A-3 alpha chain × 1 (P04439) Calreticulin × 1 (P27797) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPSN_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–428; UniProt 21–448

Protein disulfide-isomerase A3

OrganismNot specified

UniProt P30101

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 × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 25–505 Not recorded Beta-2-microglobulin × 1 (P61769) Tapasin × 1 (O15533) HLA class I histocompatibility antigen, A-3 alpha chain × 1 (P04439) Calreticulin × 1 (P27797) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDIA3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–481; UniProt 25–505

HLA class I histocompatibility antigen, A-3 alpha chain

OrganismNot specified

UniProt P04439

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 × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 25–365 Not recorded Beta-2-microglobulin × 1 (P61769) Tapasin × 1 (O15533) Protein disulfide-isomerase A3 × 1 (P30101) Calreticulin × 1 (P27797) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

53 other PDB entries and 78 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1A03_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–341; UniProt 25–365

Calreticulin

OrganismNot specified

UniProt P27797

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 × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 18–417 Not recorded Beta-2-microglobulin × 1 (P61769) Tapasin × 1 (O15533) Protein disulfide-isomerase A3 × 1 (P30101) HLA class I histocompatibility antigen, A-3 alpha chain × 1 (P04439) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-glucopyranose-(1-3)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–400; UniProt 18–417

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 6eny

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6eny
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6eny
Deposition date deposition_date2017-10-07
Structure title titleStructure of the human PLC editing module
Keywords keywordsadaptive immunity, antigen processing, chaperone, MHC class I, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.25
Radius of gyration Rg (electron density) rg_electron42.10
Forward intensity I(0) i0274282000.00
Molecular weight molecular_weight108950.0 kDa
Excluded volume excluded_volume125360 ų
Envelope volume envelope_volume271140 ų
Hydration-shell volume shell_volume56795 ų
Envelope diameter envelope_diameter139.6
Shell Rg shell_rg44.81
Envelope Rg envelope_rg40.23
Shape Rg shape_rg42.10
Total Rg total_rg42.27
Total atoms total_atoms7778
Residues n_residues1563
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 dmax136.9
Rg (real space) rg_real42.19
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real2.7430e+08
I(0) uncertainty (real space) i0_real_error4.6750e+06
Rg (reciprocal space) rg_reciprocal42.25
I(0) (reciprocal space) i0_reciprocal274300000.0000
Solution quality estimate total_estimate0.8183
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.5
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.327
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23120000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)