1hku

CtBP/BARS: a dual-function protein involved in transcription corepression and Golgi membrane fission

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

C-TERMINAL BINDING PROTEIN 3

RATTUS NORVEGICUS

UniProt Q9Z2F5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 GLYCEROL × 2 FORMIC ACID × 4 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CTBP1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–358; UniProt 1–350

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1hku
Deposition date deposition_date2003-03-11
Structure title titleCtBP/BARS: a dual-function protein involved in transcription corepression and Golgi membrane fission
Keywords keywordsTRANSCRIPTION, TRANSCRIPTION CO-REPRESSOR, TRANSCRIPTION CO-REPRESSION, ACYLTRANSFERASE, BREFELDIN A, NAD, GOLGI MEMBRANE, ACYL-COA; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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.

1hku__assembly_1__model_1

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

Download this curve (.dat)

1hku__assembly_1__model_1 | I(q)

10-2 10-1 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1hku__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)28.78 Å
Rg (electron density)28.47 Å
Total Rg29.11 Å
Atom count5236
Residues662
Excluded volume92513 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1hku__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (5)

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hkua1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.4 — Formate/glycerate dehydrogenases, NAD-domain
Domain ID domain_idd1hkua2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.12 — Formate/glycerate dehydrogenase catalytic domain-like
Family Family familyc.23.12.1 — Formate/glycerate dehydrogenases, substrate-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id1hkuA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1hkuA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain

7. Citations (2)