1dhy

KKS102 BPHC ENZYME

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

2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE

Pseudomonas sp.

UniProt P17297

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 FE (III) ION × 1 water × 1 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 8 FE (III) ION × 8 water × 8 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BPHC_PSES1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–292; UniProt 1–292

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_id1dhy
Deposition date deposition_date1995-07-07
Structure title titleKKS102 BPHC ENZYME
Keywords keywordsEXTRADIOL TYPE DIOXYGENASE, OXIDOREDUCTASE (OXYGENASE); OXIDOREDUCTASE (OXYGENASE)
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.

1dhy__assembly_1__model_1

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

Download this curve (.dat)

1dhy__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.

1dhy__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)18.82 Å
Rg (electron density)17.68 Å
Total Rg18.67 Å
Atom count2153
Residues278
Excluded volume38215 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1dhy__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1dhy__assembly_2__model_1 octameric (8) 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 (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dhya1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamilyd.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family familyd.32.1.3 — Extradiol dioxygenases
Domain ID domain_idd1dhya2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamilyd.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family familyd.32.1.3 — Extradiol dioxygenases

CATH v4.4 (2 domains)

Domain ID domain_id1dhyA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
Domain ID domain_id1dhyA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
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7. Citations (1)