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1ceo

CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN

Method: X-RAY DIFFRACTION Dmax: 67.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CELLULASE CELC

Clostridium thermocellum

UniProt P07985

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 1–343 Mutation：E140Q No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.222

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 1CEO Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CEC A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES Deposited 1995-06-07 Different mutation/modification Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–343（343 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å R-free 0.215
1CEN CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN COMPLEXED WITH CELLOHEXAOSE Deposited 1995-12-04 Different oligomeric state Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–343（343 aa）
Mutation：E140Q No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å R-free 0.246

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GUNC_CLOTM
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–343； UniProt 1–343

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 1ceo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ceo
Deposition date deposition_date1995-12-04
Structure title titleCELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN
Keywords keywordsGLYCOSYL HYDROLASE, CELLULASE, FAMILY A/5 OF GLYCOSYL HYDROLASES, CLOSTRIDIUM THERMOCELLUM, CELLULOSE DEGRADATION; CELLULOSE DEGRADATION
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_guinier21.21 Å
Radius of gyration Rg (electron density) rg_electron20.04 Å
Forward intensity I(0) i025122000.00
Molecular weight molecular_weight39329.0 kDa
Excluded volume excluded_volume49450 ų
Envelope volume envelope_volume56766 ų
Hydration-shell volume shell_volume23188 ų
Envelope diameter envelope_diameter68.6 Å
Shell Rg shell_rg27.08 Å
Envelope Rg envelope_rg20.24 Å
Shape Rg shape_rg19.99 Å
Total Rg total_rg21.08 Å
Total atoms total_atoms2782
Residues n_residues332
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 dmax67.4 Å
Rg (real space) rg_real21.08 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real2.5120e+07
I(0) uncertainty (real space) i0_real_error3.0350e+05
Rg (reciprocal space) rg_reciprocal21.11 Å
I(0) (reciprocal space) i0_reciprocal25120000.0000
Solution quality estimate total_estimate0.8969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8 Å
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5677000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.999
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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ceoa_
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 (1 domains)

Domain ID domain_id1ceoA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
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8. Citations (3)

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9. Files and Curves (10)