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1bhg

HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 135.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BETA-GLUCURONIDASE

Homo sapiens

UniProt P08236

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 21–633 Chain B； UniProt 21–633 Not recorded ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.53 Å R-free 0.310

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1BHG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3HN3 Human beta-glucuronidase at 1.7 A resolution Deposited 2009-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 21–633（613 aa）
Chain B 21–633（613 aa）
Chain D 21–633（613 aa）
Chain E 21–633（613 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 3 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 BMA beta-D-mannopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；10mM Tris-HCl pH 7.5, 15% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.70 Å R-free 0.240

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BGLR_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–613； UniProt 21–633 Author chain B； PDBConstruct 1–613； UniProt 21–633

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1bhg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bhg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bhg
Deposition date deposition_date1996-03-04
Structure title titleHUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION
Keywords keywordsLYSOSOMAL ENZYME, ACID HYDROLASE, GLYCOSIDASE; GLYCOSIDASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier40.71 Å
Radius of gyration Rg (electron density) rg_electron40.51 Å
Forward intensity I(0) i0296183000.00
Molecular weight molecular_weight144000.0 kDa
Excluded volume excluded_volume181110 ų
Envelope volume envelope_volume232820 ų
Hydration-shell volume shell_volume48196 ų
Envelope diameter envelope_diameter144.0 Å
Shell Rg shell_rg45.53 Å
Envelope Rg envelope_rg40.34 Å
Shape Rg shape_rg40.45 Å
Total Rg total_rg40.99 Å
Total atoms total_atoms10190
Residues n_residues1222
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax135.2 Å
Rg (real space) rg_real40.86 Å
Rg uncertainty (real space) rg_real_error1.22 Å
I(0) (real space) i0_real2.9620e+08
I(0) uncertainty (real space) i0_real_error4.9080e+06
Rg (reciprocal space) rg_reciprocal40.72 Å
I(0) (reciprocal space) i0_reciprocal296100000.0000
Solution quality estimate total_estimate0.8472
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.7 Å
Skewness Skewness skewness0.357
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.1950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52420000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.809; Smooth: 0.774
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1bhga1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.4 — beta-Galactosidase/glucuronidase domain
Family Family familyb.1.4.1 — beta-Galactosidase/glucuronidase domain
Domain ID domain_idd1bhga2
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.5 — beta-Galactosidase/glucuronidase, N-terminal domain
Domain ID domain_idd1bhga3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.3 — beta-glycanases
Domain ID domain_idd1bhgb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.4 — beta-Galactosidase/glucuronidase domain
Family Family familyb.1.4.1 — beta-Galactosidase/glucuronidase domain
Domain ID domain_idd1bhgb2
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.5 — beta-Galactosidase/glucuronidase, N-terminal domain
Domain ID domain_idd1bhgb3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.3 — beta-glycanases

CATH v4.4 (6 domains)

Domain ID domain_id1bhgA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id1bhgA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bhgA03
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
Domain ID domain_id1bhgB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id1bhgB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bhgB03
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
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8. Citations (2)

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9. Files and Curves (10)