3t97

Molecular Architecture of the Transport Channel of the Nuclear Pore Complex: Nup62/Nup54

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

Nuclear pore complex protein Nup54

Rattus norvegicus

UniProt P70582

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Nuclear pore glycoprotein p62 × 2 (P17955) water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUP54_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 4–65; UniProt 346–407

Nuclear pore glycoprotein p62

Rattus norvegicus

UniProt P17955

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Nuclear pore complex protein Nup54 × 1 (P70582) water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUP62_RAT
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–64; UniProt 362–425 Author chain C; PDBConstruct 1–64; UniProt 362–425

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_id3t97
Deposition date deposition_date2011-08-02
Structure title titleMolecular Architecture of the Transport Channel of the Nuclear Pore Complex: Nup62/Nup54
Keywords keywords;nucleoporin, coiled-coil, nuclear pore complex, central transport channel, alpha helical proteins, triple helix, buried polar residues, structural proteins, nucleoporins, FG repeat, nucleocytoplasmic transport, Nup58, Nup88, Nup93, karyopherin, nuclear envelope, nuclear pore membrane domain, central channel, PROTEIN TRANSPORT ;; PROTEIN TRANSPORT
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.

3t97__assembly_1__model_1

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

Download this curve (.dat)

3t97__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.

3t97__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)24.80 Å
Rg (electron density)25.16 Å
Total Rg25.40 Å
Atom count1405
Residues168
Excluded volume25075 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3t97__assembly_1__model_1 trimeric (3) 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) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3t97A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170 —
Domain ID domain_id3t97B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily490 — Single helix bin
Domain ID domain_id3t97C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170 —
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7. Citations (1)