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2og1

Crystal Structure of BphD, a C-C hydrolase from Burkholderia xenovorans LB400

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

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase

Burkholderia xenovorans

UniProt P47229

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 SULFATE ION × 8 GLYCEROL × 2 ETHANOL × 6 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

Monomer

None

Homodimer

None

Homotetramer
2og1 2pu5 2pu7 2puh 2puj 2rht 2rhw 2ri6 3v1k 3v1l 3v1m 3v1n

12 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name BPHD_BURXL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–286； UniProt 1–286 Author chain B； PDBConstruct 1–286； UniProt 1–286

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_id2og1
Deposition date deposition_date2007-01-04
Structure title titleCrystal Structure of BphD, a C-C hydrolase from Burkholderia xenovorans LB400
Keywords keywords;BphD, alpha/beta hydrolase, PCB Degradation, Meta cleavage product hydrolase, MCP hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoate hydrolase, HYDROLASE ;; HYDROLASE
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.

2og1__assembly_1__model_1

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

Download this curve (.dat)

2og1__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2og1__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）32.30 Å
Rg (electron density)31.02 Å
Total Rg31.71 Å
Atom count9054
Residues1136
Excluded volume161030 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2og1__assembly_1__model_1 tetrameric （4） 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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2og1a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.10 — Carbon-carbon bond hydrolase
Domain ID domain_idd2og1b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.10 — Carbon-carbon bond hydrolase

CATH v4.4 (2 domains)

Domain ID domain_id2og1A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id2og1B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
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7. Citations (1)