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1gu3

CBM4 structure and function

Method: X-RAY DIFFRACTION Dmax: 49.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ENDOGLUCANASE C

CELLULOMONAS FIMI

UniProt P14090

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 × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 33–181 Fragment：CARBOHYDRATE BINDING MODULE FAMILY 4, RESIDUES 1-149 beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 5；1.8M AMMONIUM SULFATE, 3% ISOPROPANOL, pH 5.00 Resolution 2.30 Å R-free 0.257

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 1GU3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CX1 SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES Deposited 1999-08-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 176–328（153 aa） Fragment：RESIDUES 176-328
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；35 K；Ionic strength (raw mmCIF value) 50mMNACL；Pressure 1
NMR sample composition 1.5 TO 2 MM CBDN2 U-15N, 13C; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5,
NMR sample composition 1.5 TO 2 MM CBDN2 U-15N; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5,
NMR sample composition 1.5 TO 2 MM CBDN2 UNLABELED; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5,
Resolution not provided
1ULO N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-07-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–184（152 aa） Fragment：N-TERMINAL CELLULOSE-BINDING DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；308 K
Resolution not provided
1ULP N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 25 STRUCTURES Deposited 1996-07-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–184（152 aa） Fragment：N-TERMINAL CELLULOSE-BINDING DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；308 K
Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GUNC_CELFI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–149； UniProt 33–181

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 1gu3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gu3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gu3
Deposition date deposition_date2002-01-22
Structure title titleCBM4 structure and function
Keywords keywordsCARBOHYDRATE-BINDING MODULE, CARBOHYDRATE BINDING MODULE, CBM, GLUCAN, CELLULOSE; CARBOHYDRATE-BINDING MODULE
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_guinier15.89 Å
Radius of gyration Rg (electron density) rg_electron14.37 Å
Forward intensity I(0) i04819570.00
Molecular weight molecular_weight15273.0 kDa
Excluded volume excluded_volume18864 ų
Envelope volume envelope_volume21165 ų
Hydration-shell volume shell_volume12621 ų
Envelope diameter envelope_diameter49.5 Å
Shell Rg shell_rg20.05 Å
Envelope Rg envelope_rg14.58 Å
Shape Rg shape_rg14.37 Å
Total Rg total_rg15.48 Å
Total atoms total_atoms1075
Residues n_residues142
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 dmax49.7 Å
Rg (real space) rg_real15.78 Å
Rg uncertainty (real space) rg_real_error0.26 Å
I(0) (real space) i0_real4.8200e+06
I(0) uncertainty (real space) i0_real_error5.5200e+04
Rg (reciprocal space) rg_reciprocal15.79 Å
I(0) (reciprocal space) i0_reciprocal4820000.0000
Solution quality estimate total_estimate0.8236
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4 Å
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.443
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha797600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1gu3a_
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.18.1.14 — CBM4/9

CATH v4.4 (1 domains)

Domain ID domain_id1gu3A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
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8. Citations (1)

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9. Files and Curves (10)