6gny

Crystal structure of the MAJIN-TERB2 heterotetrameric complex

Method: X-RAY DIFFRACTION Dmax: 74.4 Å Quality: GOOD

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

Membrane-anchored junction protein

Homo sapiens

UniProt Q3KP22

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–106 Chain C; UniProt 1–106 Not recorded Telomere repeats-binding bouquet formation protein 2 × 2 (Q8NHR7) TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12M 1,6-Hexanediol; 0.12M 1-Butanol; 0.12M 1,2-Propanediol (racemic); 0.12M 2-Propanol; 0.12M 1,4-Butanediol; 0.12M 1,3-Propanediol; 39.1 mM bicine pH 5.03; 60.9 mM Trizma pH 10.83; 18.3% w/v PEG 1000; 18.3% w/v PEG 3350; 18.3% v/v MPD Resolution 1.85 Å R-free 0.207

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAJIN_HUMAN
Isoform Q3KP22-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–108; UniProt 1–106 Author chain C; PDBConstruct 3–108; UniProt 1–106

Telomere repeats-binding bouquet formation protein 2

Homo sapiens

UniProt Q8NHR7

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 168–207 Chain D; UniProt 168–207 Not recorded Membrane-anchored junction protein × 2 (Q3KP22) TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12M 1,6-Hexanediol; 0.12M 1-Butanol; 0.12M 1,2-Propanediol (racemic); 0.12M 2-Propanol; 0.12M 1,4-Butanediol; 0.12M 1,3-Propanediol; 39.1 mM bicine pH 5.03; 60.9 mM Trizma pH 10.83; 18.3% w/v PEG 1000; 18.3% w/v PEG 3350; 18.3% v/v MPD Resolution 1.85 Å R-free 0.207

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–43; UniProt 168–207 Author chain D; PDBConstruct 4–43; UniProt 168–207

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 6gny

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6gny
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6gny
Deposition date deposition_date2018-06-01
Structure title titleCrystal structure of the MAJIN-TERB2 heterotetrameric complex
Keywords keywordsMeiosis, telomeres, complex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.53
Radius of gyration Rg (electron density) rg_electron21.40
Forward intensity I(0) i015371200.00
Molecular weight molecular_weight32047.0 kDa
Excluded volume excluded_volume41191 ų
Envelope volume envelope_volume48965 ų
Hydration-shell volume shell_volume19809 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg27.26
Envelope Rg envelope_rg21.71
Shape Rg shape_rg21.39
Total Rg total_rg22.35
Total atoms total_atoms4543
Residues n_residues273
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 dmax74.4
Rg (real space) rg_real22.53
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.5370e+07
I(0) uncertainty (real space) i0_real_error1.9880e+05
Rg (reciprocal space) rg_reciprocal22.53
I(0) (reciprocal space) i0_reciprocal15370000.0000
Solution quality estimate total_estimate0.8930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4630000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)