1na0

Design of Stable alpha-Helical Arrays from an Idealized TPR Motif

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

No usable UniProt protein identity is available for this entry.

The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.

Assembly Composition of the Current Entry

Assembly Physical composition Protein state 蛋白 / DNA / RNA / 其他Polymer Data consistency
1 Protein monomer Monomer 1 / 0 / 0 / 0 Consistent with protein count
2 Protein monomer Monomer 1 / 0 / 0 / 0 Consistent with protein count

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_id1na0
Deposition date deposition_date2002-11-26
Structure title titleDesign of Stable alpha-Helical Arrays from an Idealized TPR Motif
Keywords keywordsdesign, TPR, DE NOVO PROTEIN; DE NOVO PROTEIN
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.

1na0__assembly_1__model_1

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

Download this curve (.dat)

1na0__assembly_1__model_1 | I(q)

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

1na0__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)15.69 Å
Rg (electron density)14.83 Å
Total Rg15.85 Å
Atom count985
Residues119
Excluded volume17050 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1na0__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1na0__assembly_2__model_1 monomeric (1) 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 (8)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1na0a_
Class classk — Designed proteins
Fold Fold foldk.38 — TPR domain-based design
Superfamily Superfamily superfamilyk.38.1 — TPR domain-based design
Family Family familyk.38.1.1 — TPR domain-based design
Domain ID domain_idd1na0b_
Class classk — Designed proteins
Fold Fold foldk.38 — TPR domain-based design
Superfamily Superfamily superfamilyk.38.1 — TPR domain-based design
Family Family familyk.38.1.1 — TPR domain-based design

CATH v4.4 (2 domains)

Domain ID domain_id1na0A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id1na0B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
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7. Citations (1)