1h6p

Dimeristion domain from human TRF2

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TELOMERIC REPEAT BINDING FACTOR 2

HOMO SAPIENS

UniProt Q15554

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 MAGNESIUM ION × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q15554
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–203; UniProt 43–245 Author chain B; PDBConstruct 1–203; UniProt 43–245

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h6p
Deposition date deposition_date2001-06-20
Structure title titleDimeristion domain from human TRF2
Keywords keywordsTELOMERE BINDING, TRF2, TELOMERE, DIMERISATION, TRFH, DNA-BINDING, NUCLEAR PROTEIN; TELOMERE BINDING
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1h6p__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1h6p__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1h6p__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)23.90 Å
Rg (electron density)23.31 Å
Total Rg24.08 Å
Atom count2924
Residues376
Excluded volume52453 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1h6p__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1h6pa_
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
Domain ID domain_idd1h6pb_
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 (2 domains)

Domain ID domain_id1h6pA00
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
Domain ID domain_id1h6pB00
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
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7. Citations (3)