2bv9

HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A

Method: X-RAY DIFFRACTION Dmax: 58.2 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

ENDOGLUCANASE H

CLOSTRIDIUM THERMOCELLUM

UniProt P16218

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–304 Fragment:CATALYTIC DOMAIN, RESIDUES 26-304 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:0.3-1.2M NA FORMATE, 0.1M NA CACODYLATE BUFFERED AT PH 6.5 AND 5-20% PEG 4K Resolution 1.50 Å R-free 0.157

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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GUNH_CLOTH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–282; UniProt 26–304

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 2bv9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bv9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bv9
Deposition date deposition_date2005-06-23
Structure title titleHOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A
Keywords keywordsHYDROLASE, BETA-1 4 BETA-1 3 GLUCANASE, GLYCOSIDE HYDROLASE FAMILY 26; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.57
Radius of gyration Rg (electron density) rg_electron18.15
Forward intensity I(0) i018504100.00
Molecular weight molecular_weight32468.0 kDa
Excluded volume excluded_volume40356 ų
Envelope volume envelope_volume44430 ų
Hydration-shell volume shell_volume20029 ų
Envelope diameter envelope_diameter57.3
Shell Rg shell_rg24.82
Envelope Rg envelope_rg18.31
Shape Rg shape_rg18.12
Total Rg total_rg19.13
Total atoms total_atoms2307
Residues n_residues284
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax58.2
Rg (real space) rg_real19.42
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.8500e+07
I(0) uncertainty (real space) i0_real_error2.2120e+05
Rg (reciprocal space) rg_reciprocal19.44
I(0) (reciprocal space) i0_reciprocal18500000.0000
Solution quality estimate total_estimate0.9113
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.077
Kurtosis Kurtosis kurtosis-0.555
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3500000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2bv9a1
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_idd2bv9a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2bv9A01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases

8. Citations (1)

9. Files and Curves (10)