1aa0

FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)

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

FIBRITIN

Enterobacteria phage T4

UniProt P10104

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 3 CHLORIDE ION × 3 ZINC ION × 3 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–113; UniProt 371–483

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_id1aa0
Deposition date deposition_date1997-01-18
Structure title titleFIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)
Keywords keywordsBACTERIOPHAGE T4, FIBRITIN, STRUCTURAL PROTEIN, BACTERIOPHAGE ASSEMBLY, ATTACHMENT PROTEIN; ATTACHMENT 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.

1aa0__assembly_1__model_1

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

Download this curve (.dat)

1aa0__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.

1aa0__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)36.89 Å
Rg (electron density)39.17 Å
Total Rg38.85 Å
Atom count3112
Residues339
Excluded volume43953 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1aa0__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 (4)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1aa0a_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.17 — Fibritin
Family Family familyh.1.17.1 — Fibritin

CATH v4.4 (1 domains)

Domain ID domain_id1aa0A00
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 superfamily320 — 6-Phosphogluconate Dehydrogenase, domain 3
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7. Citations (3)