3eqo

Crystal structure of beta-1,3-glucanase from Phanerochaete chrysosporium (Lam55A) gluconolactone complex

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

Glucan 1,3-beta-glucosidase

Phanerochaete chrysosporium

UniProt Q2Z1W1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Other combination Monomer Protein 1 其他Polymer 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ZINC ION × 1 D-glucono-1,5-lactone × 1 water × 1 Consistent with protein count
2 Other combination Monomer Protein 1 其他Polymer 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ZINC ION × 1 D-glucono-1,5-lactone × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q2Z1W1_PHACH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–758; UniProt 27–778 Author chain B; PDBConstruct 7–758; UniProt 27–778

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_id3eqo
Deposition date deposition_date2008-10-01
Structure title titleCrystal structure of beta-1,3-glucanase from Phanerochaete chrysosporium (Lam55A) gluconolactone complex
Keywords keywordstandem beta-helix domains, Glycosidase, 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.

3eqo__assembly_1__model_1

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

Download this curve (.dat)

3eqo__assembly_1__model_1 | I(q)

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

3eqo__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)25.51 Å
Rg (electron density)24.12 Å
Total Rg25.01 Å
Atom count5663
Residues752
Excluded volume99116 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3eqo__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3eqo__assembly_2__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) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3eqoA01
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily10 — Single-stranded right-handed beta-helix, Pectin lyase-like
Domain ID domain_id3eqoA02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily10 — Single-stranded right-handed beta-helix, Pectin lyase-like
Domain ID domain_id3eqoB01
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily10 — Single-stranded right-handed beta-helix, Pectin lyase-like
Domain ID domain_id3eqoB02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily10 — Single-stranded right-handed beta-helix, Pectin lyase-like
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7. Citations (2)