2b56

Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei

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

RNA editing complex protein MP57

Trypanosoma brucei

UniProt Q86MV5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 MAGNESIUM ION × 1 ;URIDINE 5'-TRIPHOSPHATE ; × 1 URIDINE-5'-MONOPHOSPHATE × 2 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q86MV5_9TRYP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–468; UniProt 20–487

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_id2b56
Deposition date deposition_date2005-09-27
Structure title titleStructural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei
Keywords keywordsTbRET2, TUTase, RNA Editing, transferase, trypanosoma brucei, TRANSFERASE-RNA BINDING PROTEIN COMPLEX; TRANSFERASE/RNA BINDING 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.

2b56__assembly_1__model_1

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

Download this curve (.dat)

2b56__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.

2b56__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)25.33 Å
Rg (electron density)24.66 Å
Total Rg25.31 Å
Atom count3637
Residues444
Excluded volume64095 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2b56__assembly_1__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 (5)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2b56a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.218 — Nucleotidyltransferase
Superfamily Superfamily superfamilyd.218.1 — Nucleotidyltransferase
Family Family familyd.218.1.10 — RNA editing terminal uridyl transferase 2, RET2, catalytic domain
Domain ID domain_idd2b56a2
Class classa — All alpha proteins
Fold Fold folda.160 — PAP/OAS1 substrate-binding domain
Superfamily Superfamily superfamilya.160.1 — PAP/OAS1 substrate-binding domain
Family Family familya.160.1.4 — RNA editing terminal uridyl transferase 2, RET2, domain 2

CATH v4.4 (3 domains)

Domain ID domain_id2b56A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1410 — Poly(a)-polymerase, middle domain
Homologous superfamily homologous superfamily10 —
Domain ID domain_id2b56A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology460 — Beta Polymerase; domain 2
Homologous superfamily homologous superfamily50 —
Domain ID domain_id2b56A03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1970 —
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7. Citations (1)