6gnx

Crystal structure of the MAJIN-TERB2 heterotetrameric complex - selenomethionine derivative

Method: X-RAY DIFFRACTION Dmax: 75.8 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 1–112 Chain C; UniProt 1–112 Non-standard monomer:Yes (specific site not provided by mmCIF) Telomere repeats-binding bouquet formation protein 2 × 2 (Q8NHR7) 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, 55.5 mM MES pH 3.11, 44.5 mM imidazole pH 10.23; 12.5% w/v PEG 1000; 12.5% w/v PEG 3350; 12.5% v/v MPD Resolution 2.90 Å R-free 0.304

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 3–114; UniProt 1–112 Author chain C; PDBConstruct 3–114; UniProt 1–112

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 169–220 Chain D; UniProt 169–220 Non-standard monomer:Yes (specific site not provided by mmCIF) Membrane-anchored junction protein × 2 (Q3KP22) 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, 55.5 mM MES pH 3.11, 44.5 mM imidazole pH 10.23; 12.5% w/v PEG 1000; 12.5% w/v PEG 3350; 12.5% v/v MPD Resolution 2.90 Å R-free 0.304

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 4–55; UniProt 169–220 Author chain D; PDBConstruct 4–55; UniProt 169–220

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 6gnx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gnx
Deposition date deposition_date2018-06-01
Structure title titleCrystal structure of the MAJIN-TERB2 heterotetrameric complex - selenomethionine derivative
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_guinier22.40
Radius of gyration Rg (electron density) rg_electron21.32
Forward intensity I(0) i014334000.00
Molecular weight molecular_weight31046.0 kDa
Excluded volume excluded_volume39824 ų
Envelope volume envelope_volume47999 ų
Hydration-shell volume shell_volume19442 ų
Envelope diameter envelope_diameter72.6
Shell Rg shell_rg27.34
Envelope Rg envelope_rg21.74
Shape Rg shape_rg21.32
Total Rg total_rg22.23
Total atoms total_atoms4369
Residues n_residues258
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_real22.42
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.4330e+07
I(0) uncertainty (real space) i0_real_error1.9840e+05
Rg (reciprocal space) rg_reciprocal22.42
I(0) (reciprocal space) i0_reciprocal14330000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3763000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)