2jvb

Solution Structure of Catalytic Domain of yDcp2

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

mRNA-decapping enzyme subunit 2

Saccharomyces cerevisiae

UniProt P53550

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DCP2_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–146; UniProt 100–245

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_id2jvb
Deposition date deposition_date2007-09-16
Structure title titleSolution Structure of Catalytic Domain of yDcp2
Keywords keywords;Dcp2, mRNA decay, decapping, Cytoplasm, Hydrolase, Manganese, Metal-binding, mRNA processing, Nonsense-mediated mRNA decay, Nucleus, Phosphorylation, RNA-binding ;; HYDROLASE
Experimental Method methodSOLUTION NMR
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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.

2jvb__assembly_1__model_8

Assembly 1 · Model 8 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2jvb__assembly_1__model_8 | I(q)

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

2jvb__assembly_1__model_8 | 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)17.07 Å
Rg (electron density)15.50 Å
Total Rg16.78 Å
Atom count2446
Residues146
Excluded volume21844 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2jvb__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2jvb__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2jvb__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2jvb__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2jvb__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2jvb__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2jvb__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2jvb__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2jvb__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2jvb__assembly_1__model_10 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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2jvba_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.113 — Nudix
Superfamily Superfamily superfamilyd.113.1 — Nudix
Family Family familyd.113.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2jvbA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology79 — Nucleoside Triphosphate Pyrophosphohydrolase
Homologous superfamily homologous superfamily10 — Nucleoside Triphosphate Pyrophosphohydrolase
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7. Citations (1)