1v59

Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+

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

Dihydrolipoamide dehydrogenase

OrganismNot specified

UniProt P09624

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 PHOSPHATE ION × 1 FLAVIN-ADENINE DINUCLEOTIDE × 2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DLDH_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–478; UniProt 22–499 Author chain B; PDBConstruct 1–478; UniProt 22–499

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_id1v59
Deposition date deposition_date2003-11-21
Structure title titleCrystal structure of yeast lipoamide dehydrogenase complexed with NAD+
Keywords keywords;2-oxoacid dehydroganese complex, pyruvate dehydrogenase complex, lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, pyridine nucleotide-disulphide oxidoreductase, NAD+, OXIDOREDUCTASE ;; 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.

1v59__assembly_1__model_1

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

Download this curve (.dat)

1v59__assembly_1__model_1 | I(q)

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

1v59__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)31.10 Å
Rg (electron density)30.54 Å
Total Rg31.14 Å
Atom count7392
Residues956
Excluded volume131610 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1v59__assembly_1__model_1 dimeric (2) 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) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1v59a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1v59a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1v59a3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamilyd.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Family Family familyd.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Domain ID domain_idd1v59b1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1v59b2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1v59b3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamilyd.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Family Family familyd.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain

CATH v4.4 (6 domains)

Domain ID domain_id1v59A01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1v59A02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1v59A03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily30 — FAD/NAD-linked reductase, C-terminal dimerisation domain
Domain ID domain_id1v59B01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1v59B02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1v59B03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily30 — FAD/NAD-linked reductase, C-terminal dimerisation domain
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7. Citations (1)