1rp4

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

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

Hypothetical 65.0 kDa protein in COX14-COS3 intergenic region precursor

Saccharomyces cerevisiae

UniProt Q03103

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 CADMIUM ION × 2 1-ETHYL-PYRROLIDINE-2,5-DIONE × 1 FLAVIN-ADENINE DINUCLEOTIDE × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ERO1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–386; UniProt 56–424

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_id1rp4
Deposition date deposition_date2003-12-03
Structure title titleStructure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
Keywords keywordsflavoenzyme, disulfide bonds, CXXCXXC, 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.

1rp4__assembly_1__model_1

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

Download this curve (.dat)

1rp4__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.

1rp4__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)21.93 Å
Rg (electron density)20.74 Å
Total Rg21.60 Å
Atom count3067
Residues367
Excluded volume54377 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1rp4__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) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1rp4a1
Class classa — All alpha proteins
Fold Fold folda.227 — ERO1-like
Superfamily Superfamily superfamilya.227.1 — ERO1-like
Family Family familya.227.1.1 — ERO1-like
Domain ID domain_idd1rp4a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1rp4a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
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7. Citations (1)