2j09

Thermus DNA photolyase with FMN antenna chromophore

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

DEOXYRIBODIPYRIMIDINE PHOTO-LYASE

THERMUS THERMOPHILUS

UniProt P61497

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 CHLORIDE ION × 1 FLAVIN-ADENINE DINUCLEOTIDE × 1 FLAVIN MONONUCLEOTIDE × 1 PHOSPHATE ION × 2 water × 1 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 2 CHLORIDE ION × 2 FLAVIN-ADENINE DINUCLEOTIDE × 2 FLAVIN MONONUCLEOTIDE × 2 PHOSPHATE ION × 4 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PHR_THET8
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–420; UniProt 1–420

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_id2j09
Deposition date deposition_date2006-08-01
Structure title titleThermus DNA photolyase with FMN antenna chromophore
Keywords keywordsLYASE, FLAVOPROTEIN, DNA REPAIR; LYASE
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.

2j09__assembly_1__model_1

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

Download this curve (.dat)

2j09__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.

2j09__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)23.08 Å
Rg (electron density)22.31 Å
Total Rg23.28 Å
Atom count3488
Residues419
Excluded volume61526 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2j09__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 2j09__assembly_2__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 (6)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2j09a1
Class classa — All alpha proteins
Fold Fold folda.99 — Cryptochrome/photolyase FAD-binding domain
Superfamily Superfamily superfamilya.99.1 — Cryptochrome/photolyase FAD-binding domain
Family Family familya.99.1.1 — Cryptochrome/photolyase FAD-binding domain
Domain ID domain_idd2j09a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.28 — Cryptochrome/photolyase, N-terminal domain
Superfamily Superfamily superfamilyc.28.1 — Cryptochrome/photolyase, N-terminal domain
Family Family familyc.28.1.1 — Cryptochrome/photolyase, N-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id2j09A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily620 — HUPs
Domain ID domain_id2j09A02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily80 —
Domain ID domain_id2j09A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology579 — DNA Cyclobutane Dipyrimidine Photolyase, subunit A; domain 3
Homologous superfamily homologous superfamily10 — DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3
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7. Citations (1)