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3cel

ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE

Method: X-RAY DIFFRACTION Dmax: 66.9 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I

Hypocrea jecorina

UniProt P00725

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 19–451 Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434 Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF) beta-D-glucopyranose-(1-4)-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CD CADMIUM ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；50 MM MES PH 6.0, 5% MONOMETHYL ETHER PEG 5000, 5 MM CDCL2, 1 MM CELLOBIOSE Resolution 2.00 Å R-free 0.256

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 3CEL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CEL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI Deposited 1994-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 19–451（433 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BGC beta-D-glucopyranose × 1 CA CALCIUM ION × 1 IBZ 2-IODOBENZYLTHIO GROUP × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1CEL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI Deposited 1994-05-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 19–451（433 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 IBZ 2-IODOBENZYLTHIO GROUP × 1 GLC alpha-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1Q2E CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE Deposited 2003-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 18–451（434 aa） Fragment：CATALYTIC DOMAIN 1-434
Mutation：245-252 DELETION Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；PEG 5000, TRIS-HCL, ETHYLENE GLYCOL, CALCIUM CHLORIDE, SODIUM ACETATE, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.75 Å R-free 0.239
1Q2E CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE Deposited 2003-07-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain B 18–451（434 aa） Fragment：CATALYTIC DOMAIN 1-434
Mutation：245-252 DELETION Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；PEG 5000, TRIS-HCL, ETHYLENE GLYCOL, CALCIUM CHLORIDE, SODIUM ACETATE, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.75 Å R-free 0.239
5CEL CBH1 (E212Q) CELLOTETRAOSE COMPLEX Deposited 1997-09-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK SOLUTION CONTAINED 0.1 M MES (PH 6.0), 20% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, 20% GLYCEROL AND 0.005 M CELLOTETRAOSE. THE AXES OF THE CRYO-COOLED CRYSTALS ARE SYSTEMATICALLY SHORTER THAN THOSE OF CRYSTALS COLLECTED AT ROOM TEMPERATURE. IN ORDER TO KEEP THE SAME INDEXING AS IN PREVIOUS ROOM-TEMPERATURE DATA SETS, THE LONGER A-AXIS IS LISTED BEFORE THE SHORTER B-AXIS., vapor diffusion - hanging drop
Resolution 1.90 Å R-free 0.240
6CEL CBH1 (E212Q) CELLOPENTAOSE COMPLEX Deposited 1997-09-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation：E212Q Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK SOLUTION CONTAINED 0.1 M MES (PH 6.0), 20% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, 15% GLYCEROL AND 0.004 M CELLOTETRAOSE. THE AXES OF THE CRYO-COOLED CRYSTALS ARE SYSTEMATICALLY SHORTER THAN THOSE OF CRYSTALS COLLECTED AT ROOM TEMPERATURE. IN ORDER TO KEEP THE SAME INDEXING AS IN PREVIOUS ROOM-TEMPERATURE DATA SETS, THE LONGER A-AXIS IS LISTED BEFORE THE SHORTER B-AXIS., vapor diffusion - hanging drop
Resolution 1.70 Å R-free 0.235
7CEL CBH1 (E217Q) IN COMPLEX WITH CELLOHEXAOSE AND CELLOBIOSE Deposited 1997-09-24 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric
Chain A 19–451（433 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 1 - 434
Mutation：E217Q Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE., vapor diffusion - hanging drop
Resolution 1.90 Å R-free 0.215

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GUX1_TRIRE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–434； UniProt 19–451

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 3cel

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cel
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3cel
Deposition date deposition_date1996-08-24
Structure title titleACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE
Keywords keywordsCELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE, GLYCOPROTEIN; HYDROLASE
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_guinier21.78 Å
Radius of gyration Rg (electron density) rg_electron20.55 Å
Forward intensity I(0) i044105800.00
Molecular weight molecular_weight47131.0 kDa
Excluded volume excluded_volume56726 ų
Envelope volume envelope_volume64877 ų
Hydration-shell volume shell_volume25622 ų
Envelope diameter envelope_diameter68.8 Å
Shell Rg shell_rg28.00 Å
Envelope Rg envelope_rg20.67 Å
Shape Rg shape_rg20.48 Å
Total Rg total_rg21.53 Å
Total atoms total_atoms3266
Residues n_residues433
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 dmax66.9 Å
Rg (real space) rg_real21.62 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real4.4110e+07
I(0) uncertainty (real space) i0_real_error5.2940e+05
Rg (reciprocal space) rg_reciprocal21.65 Å
I(0) (reciprocal space) i0_reciprocal44110000.0000
Solution quality estimate total_estimate0.7167
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.0 Å
Skewness Skewness skewness0.144
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.3650 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7757000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 0.207; Positv: 1.000; Valcen: 0.989; Smooth: 0.965
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3cela_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.10 — Glycosyl hydrolase family 7 catalytic core

CATH v4.4 (1 domains)

Domain ID domain_id3celA00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily10 — Glycoside hydrolase, family 7, domain
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8. Citations (3)

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9. Files and Curves (10)