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1cx1

SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES

Method: SOLUTION NMR Dmax: 46.3 Å Quality: EXCELLENT
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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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 176–328 Fragment：RESIDUES 176-328 No other associated polymer 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

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 1CX1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1GU3 CBM4 structure and function Deposited 2002-01-22 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 33–181（149 aa） Fragment：CARBOHYDRATE BINDING MODULE FAMILY 4, RESIDUES 1-149
Not recorded No recorded non-water small molecule 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
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 experimental conditions 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 experimental conditions 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 1–153； UniProt 176–328

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 1cx1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cx1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cx1
Deposition date deposition_date1999-08-27
Structure title titleSECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES
Keywords keywordsCELLULOSE-BINDING DOMAIN, CELLOOLIGOSACHARIDES, CELLULASE, PROTEIN- CARBOHYDRATE INTERACTION, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.56 Å
Radius of gyration Rg (electron density) rg_electron15.04 Å
Forward intensity I(0) i01733950000.00
Molecular weight molecular_weight348860.0 kDa
Excluded volume excluded_volume432570 ų
Envelope volume envelope_volume32978 ų
Hydration-shell volume shell_volume16590 ų
Envelope diameter envelope_diameter52.5 Å
Shell Rg shell_rg22.70 Å
Envelope Rg envelope_rg16.86 Å
Shape Rg shape_rg15.02 Å
Total Rg total_rg15.22 Å
Total atoms total_atoms47608
Residues n_residues3366
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 dmax46.3 Å
Rg (real space) rg_real15.47 Å
Rg uncertainty (real space) rg_real_error0.22 Å
I(0) (real space) i0_real1.7340e+09
I(0) uncertainty (real space) i0_real_error1.9800e+07
Rg (reciprocal space) rg_reciprocal15.48 Å
I(0) (reciprocal space) i0_reciprocal1734000000.0000
Solution quality estimate total_estimate0.9145
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.8 Å
Skewness Skewness skewness0.089
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha286800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.991
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cx1a1
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
Domain ID domain_idd1cx1a2
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_id1cx1A00
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 (3)

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9. Files and Curves (10)