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7c89

Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant modified with 2-bromoacetophenone(Ph@ApPrx*)

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

Peroxiredoxin

Aeropyrum pernix K1

UniProt Q9Y9L0

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 10 CITRATE ANION × 10 2-bromanyl-1-phenyl-ethanone × 10 water × 10 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer
1x0r 1x0r 1x0r 1x0r 1x0r 5xbs 5xbs 6krr 6krr

9 assemblies

Homotetramer

None

Other homooligomers
1x0r 2cv4 2e2g 2e2m 2nvl 2zct 3a2v 3a2w 3a2x 3a5w 6krk 6krm

19 assemblies; showing the first 12

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name TDXH_AERPE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–250； UniProt 1–250 Author chain B； PDBConstruct 1–250； UniProt 1–250 Author chain C； PDBConstruct 1–250； UniProt 1–250 Author chain D； PDBConstruct 1–250； UniProt 1–250 Author chain E； PDBConstruct 1–250； UniProt 1–250 Author chain F； PDBConstruct 1–250； UniProt 1–250 Author chain G； PDBConstruct 1–250； UniProt 1–250 Author chain H； PDBConstruct 1–250； UniProt 1–250 Author chain I； PDBConstruct 1–250； UniProt 1–250 Author chain J； PDBConstruct 1–250； UniProt 1–250

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_id7c89
Deposition date deposition_date2020-05-29
Structure title titlePeroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant modified with 2-bromoacetophenone(Ph@ApPrx*)
Keywords keywordsPeroxiredoxin, 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.

7c89__assembly_1__model_1

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

Download this curve (.dat)

7c89__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7c89__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）51.53 Å
Rg (electron density)50.59 Å
Total Rg50.83 Å
Atom count19900
Residues2440
Excluded volume354090 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7c89__assembly_1__model_1 decameric （10） 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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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd7c89a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89d_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89e_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89f_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89g_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89h_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89i_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
Domain ID domain_idd7c89j_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.10 — Glutathione peroxidase-like
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7. Citations (1)