3blw

Yeast Isocitrate Dehydrogenase with Citrate and AMP Bound in the Regulatory Subunits

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

Isocitrate dehydrogenase [NAD] subunit 1

Saccharomyces cerevisiae

UniProt P28834

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 Isocitrate dehydrogenase [NAD] subunit 2 × 4 (P28241) CITRATE ANION × 4 ADENOSINE MONOPHOSPHATE × 4 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 8 Isocitrate dehydrogenase [NAD] subunit 2 × 4 (P28241) CITRATE ANION × 4 ADENOSINE MONOPHOSPHATE × 4 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 2 × 2 (P28241) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 2 × 2 (P28241) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
5 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 2 × 2 (P28241) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
6 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 2 × 2 (P28241) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name IDH1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–349; UniProt 12–360 Author chain C; PDBConstruct 1–349; UniProt 12–360 Author chain E; PDBConstruct 1–349; UniProt 12–360 Author chain G; PDBConstruct 1–349; UniProt 12–360 Author chain I; PDBConstruct 1–349; UniProt 12–360 Author chain K; PDBConstruct 1–349; UniProt 12–360 Author chain M; PDBConstruct 1–349; UniProt 12–360 Author chain O; PDBConstruct 1–349; UniProt 12–360

Isocitrate dehydrogenase [NAD] subunit 2

Saccharomyces cerevisiae

UniProt P28241

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 Isocitrate dehydrogenase [NAD] subunit 1 × 4 (P28834) CITRATE ANION × 4 ADENOSINE MONOPHOSPHATE × 4 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 8 Isocitrate dehydrogenase [NAD] subunit 1 × 4 (P28834) CITRATE ANION × 4 ADENOSINE MONOPHOSPHATE × 4 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 1 × 2 (P28834) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 1 × 2 (P28834) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
5 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 1 × 2 (P28834) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count
6 Protein heterocomplex Heteromer Protein 4 Isocitrate dehydrogenase [NAD] subunit 1 × 2 (P28834) CITRATE ANION × 2 ADENOSINE MONOPHOSPHATE × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name IDH2_YEAST
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–354; UniProt 16–369 Author chain D; PDBConstruct 1–354; UniProt 16–369 Author chain F; PDBConstruct 1–354; UniProt 16–369 Author chain H; PDBConstruct 1–354; UniProt 16–369 Author chain J; PDBConstruct 1–354; UniProt 16–369 Author chain L; PDBConstruct 1–354; UniProt 16–369 Author chain N; PDBConstruct 1–354; UniProt 16–369 Author chain P; PDBConstruct 1–354; UniProt 16–369

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_id3blw
Deposition date deposition_date2007-12-11
Structure title titleYeast Isocitrate Dehydrogenase with Citrate and AMP Bound in the Regulatory Subunits
Keywords keywords;TCA cycle, oxidative metabolism, allostery, dehydrogenase, decarboxylase, Allosteric enzyme, Magnesium, Manganese, Metal-binding, Mitochondrion, NAD, Oxidoreductase, RNA-binding, Transit peptide, Tricarboxylic acid cycle, Phosphoprotein ;; OXIDOREDUCTASE
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.

3blw__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3blw__assembly_3__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3blw__assembly_3__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)37.93 Å
Rg (electron density)37.26 Å
Total Rg37.63 Å
Atom count10428
Residues1361
Excluded volume186190 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3blw__assembly_1__model_1 octameric (8) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3blw__assembly_2__model_1 octameric (8) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 3blw__assembly_3__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 3blw__assembly_4__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
5 1 3blw__assembly_5__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
6 1 3blw__assembly_6__model_1 tetrameric (4) 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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7. Citations (1)