1dut

FIV DUTP PYROPHOSPHATASE

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

DUTP PYROPHOSPHATASE

Feline immunodeficiency virus

UniProt P16088

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name POL_FIVPE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–133; UniProt 711–843 Author chain B; PDBConstruct 1–133; UniProt 711–843

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_id1dut
Deposition date deposition_date1996-09-15
Structure title titleFIV DUTP PYROPHOSPHATASE
Keywords keywords;POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE, ENDONUCLEASE, RNA-DIRECTED DNA POLYMERASE, NUCLEOTIDE METABOLISM, ACID ANHYDRIDE HYDROLASE ;; ASPARTYL PROTEASE
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.

1dut__assembly_1__model_1

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

Download this curve (.dat)

1dut__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.

1dut__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)21.12 Å
Rg (electron density)19.77 Å
Total Rg20.81 Å
Atom count2662
Residues351
Excluded volume48825 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1dut__assembly_1__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1dut__assembly_2__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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1duta_
Class classb — All beta proteins
Fold Fold foldb.85 — beta-clip
Superfamily Superfamily superfamilyb.85.4 — dUTPase-like
Family Family familyb.85.4.1 — dUTPase-like
Domain ID domain_idd1dutb_
Class classb — All beta proteins
Fold Fold foldb.85 — beta-clip
Superfamily Superfamily superfamilyb.85.4 — dUTPase-like
Family Family familyb.85.4.1 — dUTPase-like

CATH v4.4 (2 domains)

Domain ID domain_id1dutA00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology40 — Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
Homologous superfamily homologous superfamily10 — Deoxyuridine triphosphatase (dUTPase)
Domain ID domain_id1dutB00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology40 — Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
Homologous superfamily homologous superfamily10 — Deoxyuridine triphosphatase (dUTPase)
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7. Citations (1)