1h6o

Dimerisation domain from human TRF1

Method: X-RAY DIFFRACTION Dmax: 75.9 Å Quality: REASONABLE

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

TELOMERIC REPEAT BINDING FACTOR 1

HOMO SAPIENS

UniProt P54274

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 62–265 Fragment:DIMERISATION DOMAIN RESIDUES 63-265 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;PH6, 5-15% GLYCEROL, 1-5 MM MAGNESIUM ACETATE, 1 % PEG 8000, pH 6.00 Resolution 2.90 Å R-free 0.303

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.

57 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–204; UniProt 62–265

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 1h6o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h6o
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1h6o
Deposition date deposition_date2001-06-20
Structure title titleDimerisation domain from human TRF1
Keywords keywordsTELOMERE BINDING, TRF1, TELOMERE, DIMERISATION, TRFH, DNA-BINDING, NUCLEAR PROTEIN; TELOMERE BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.40
Radius of gyration Rg (electron density) rg_electron18.70
Forward intensity I(0) i08378560.00
Molecular weight molecular_weight21000.0 kDa
Excluded volume excluded_volume26161 ų
Envelope volume envelope_volume32077 ų
Hydration-shell volume shell_volume15411 ų
Envelope diameter envelope_diameter77.7
Shell Rg shell_rg23.81
Envelope Rg envelope_rg19.38
Shape Rg shape_rg18.74
Total Rg total_rg19.42
Total atoms total_atoms1475
Residues n_residues195
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 dmax75.9
Rg (real space) rg_real19.53
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real8.3790e+06
I(0) uncertainty (real space) i0_real_error1.3070e+05
Rg (reciprocal space) rg_reciprocal19.51
I(0) (reciprocal space) i0_reciprocal8378000.0000
Solution quality estimate total_estimate0.6875
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.625
Kurtosis Kurtosis kurtosis0.366
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1777000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.442; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.612; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1h6oa_
Class classa — All alpha proteins
Fold Fold folda.146 — Telomeric repeat binding factor (TRF) dimerisation domain
Superfamily Superfamily superfamilya.146.1 — Telomeric repeat binding factor (TRF) dimerisation domain
Family Family familya.146.1.1 — Telomeric repeat binding factor (TRF) dimerisation domain

CATH v4.4 (1 domains)

Domain ID domain_id1h6oA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily210 — Telomere repeat-binding factor, dimerisation domain

8. Citations (2)

9. Files and Curves (10)