SAXSdb — 1mac

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

1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE

Paenibacillus macerans

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 28–239	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.30 Å
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 28–239	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.30 Å

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 1MAC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AJK CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-84 Deposited 1997-05-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 107–237（131 aa）	Not recorded	CA CALCIUM ION × 1 PO4 PHOSPHATE ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；SITTING DROP METHOD: A SOLUTION OF 12 MG OF PROTEIN PER ML IN 10 MM HEPES, PH 7.0, 2 MM CA-CHLORIDE, MIXED WITH AN EQUAL VOLUME OF 50 MM K-PHOSPHATE, PH 7.0 AND 20% (BY WEIGHT) PEG 8000, vapor diffusion - sitting drop	Resolution 1.80 Å R-free 0.219
1AJK CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-84 Deposited 1997-05-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 107–237（131 aa）	Not recorded	CA CALCIUM ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；SITTING DROP METHOD: A SOLUTION OF 12 MG OF PROTEIN PER ML IN 10 MM HEPES, PH 7.0, 2 MM CA-CHLORIDE, MIXED WITH AN EQUAL VOLUME OF 50 MM K-PHOSPHATE, PH 7.0 AND 20% (BY WEIGHT) PEG 8000, vapor diffusion - sitting drop	Resolution 1.80 Å R-free 0.219
1AJO CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-127 Deposited 1997-05-07	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–149（149 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；HANGING DROP METHOD: A SOLUTION OF 18 MG OF PROTEIN PER ML IN 20 MM TRIS/HCL, PH 9.0, 2 MM CA-CHLORIDE, MIXED WITH AN EQUAL VOLUME OF 0.1 M IMIDAZOLE, PH7.5,2 MM CA-CHLORIDE, 10% (BY WEIGHT) PEG 8000 AND 8% (BY VOL.) ETHYLENE GLYCOL., vapor diffusion - hanging drop	Resolution 2.07 Å R-free 0.235
1AJO CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-127 Deposited 1997-05-07	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–149（149 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；HANGING DROP METHOD: A SOLUTION OF 18 MG OF PROTEIN PER ML IN 20 MM TRIS/HCL, PH 9.0, 2 MM CA-CHLORIDE, MIXED WITH AN EQUAL VOLUME OF 0.1 M IMIDAZOLE, PH7.5,2 MM CA-CHLORIDE, 10% (BY WEIGHT) PEG 8000 AND 8% (BY VOL.) ETHYLENE GLYCOL., vapor diffusion - hanging drop	Resolution 2.07 Å R-free 0.235
1AXK ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1 Deposited 1997-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 82–237（156 aa） Fragment：FUSION OF 1,3-1,4-BETA-GLUCANASE DOMAIN AND 1,4-BETA-XYLANASE DOMAIN Chain B 82–237（156 aa） Fragment：FUSION OF 1,3-1,4-BETA-GLUCANASE DOMAIN AND 1,4-BETA-XYLANASE DOMAIN	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.10 Å R-free 0.224
1CPM NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS Deposited 1994-03-11	Different construct Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 82–237（156 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1CPN NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS Deposited 1994-03-11	Different construct Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 82–237（156 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1GLH CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY Deposited 1994-11-25	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–239（214 aa）	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.225
1U0A Crystal structure of the engineered beta-1,3-1,4-endoglucanase H(A16-M) in complex with beta-glucan tetrasaccharide Deposited 2004-07-13	Different construct 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 40–237（198 aa）	Mutation：E105Q, E109Q	CA CALCIUM ION × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；293 K；25% (v/v) PEG Monomethyl Ether 550, 0.01 M Zinc Sulfate heptahydrate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50	Resolution 1.64 Å R-free 0.197
1U0A Crystal structure of the engineered beta-1,3-1,4-endoglucanase H(A16-M) in complex with beta-glucan tetrasaccharide Deposited 2004-07-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 40–237（198 aa）	Mutation：E105Q, E109Q	CA CALCIUM ION × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；293 K；25% (v/v) PEG Monomethyl Ether 550, 0.01 M Zinc Sulfate heptahydrate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50	Resolution 1.64 Å R-free 0.197
1U0A Crystal structure of the engineered beta-1,3-1,4-endoglucanase H(A16-M) in complex with beta-glucan tetrasaccharide Deposited 2004-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 40–237（198 aa）	Mutation：E105Q, E109Q	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；293 K；25% (v/v) PEG Monomethyl Ether 550, 0.01 M Zinc Sulfate heptahydrate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50	Resolution 1.64 Å R-free 0.197
1U0A Crystal structure of the engineered beta-1,3-1,4-endoglucanase H(A16-M) in complex with beta-glucan tetrasaccharide Deposited 2004-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain D 40–237（198 aa）	Mutation：E105Q, E109Q	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；293 K；25% (v/v) PEG Monomethyl Ether 550, 0.01 M Zinc Sulfate heptahydrate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50	Resolution 1.64 Å R-free 0.197
1U0A Crystal structure of the engineered beta-1,3-1,4-endoglucanase H(A16-M) in complex with beta-glucan tetrasaccharide Deposited 2004-07-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 40–237（198 aa） Chain B 40–237（198 aa） Chain C 40–237（198 aa） Chain D 40–237（198 aa）	Mutation：E105Q, E109Q Mutation：E105Q, E109Q Mutation：E105Q, E109Q Mutation：E105Q, E109Q	CA CALCIUM ION × 4 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；293 K；25% (v/v) PEG Monomethyl Ether 550, 0.01 M Zinc Sulfate heptahydrate, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50	Resolution 1.64 Å R-free 0.197
2AYH CRYSTAL AND MOLECULAR STRUCTURE AT 1.6 ANGSTROMS RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M) Deposited 1995-02-02	Different construct Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–239（214 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GUB_PAEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–212； UniProt 28–239 Author chain B； PDBConstruct 1–212； UniProt 28–239

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1mac
Deposition date deposition_date	1994-12-22
Structure title title	CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE
Keywords keywords	HYDROLASE (GLUCANASE); HYDROLASE (GLUCANASE)
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	27.98 Å
Radius of gyration Rg (electron density) rg_electron	27.36 Å
Forward intensity I(0) i0	36853000.00
Molecular weight molecular_weight	47685.0 kDa
Excluded volume excluded_volume	59563 Å³
Envelope volume envelope_volume	70406 Å³
Hydration-shell volume shell_volume	22561 Å³
Envelope diameter envelope_diameter	96.7 Å
Shell Rg shell_rg	33.02 Å
Envelope Rg envelope_rg	27.28 Å
Shape Rg shape_rg	27.32 Å
Total Rg total_rg	28.09 Å
Total atoms total_atoms	3382
Residues n_residues	424
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	92.8 Å
Rg (real space) rg_real	28.24 Å
Rg uncertainty (real space) rg_real_error	0.76 Å
I(0) (real space) i0_real	3.6850e+07
I(0) uncertainty (real space) i0_real_error	5.4540e+05
Rg (reciprocal space) rg_reciprocal	28.17 Å
I(0) (reciprocal space) i0_reciprocal	36850000.0000
Solution quality estimate total_estimate	0.6007
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	24.4 Å
Skewness Skewness skewness	0.435
Kurtosis Kurtosis kurtosis	-0.659
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8418000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.641; Stabil: 1.000; Sysdev: 0.075; Positv: 1.000; Valcen: 0.728; Smooth: 0.928

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE
Molecular weight formula_weight	23826.2 kDa
EC 编号 ec_number	3.2.1.73
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3557

GSVFWEPLSYFNPSTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLGLTSSAYNKFDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHGTQWDEIDIEFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFDWQPGYIKWYVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGANPLYAEYDWVKYTSN

来源 Source

来源生物 organism	Paenibacillus macerans
NCBI Class编号 ncbi_taxonomy_id	44252
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	175

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1maca_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.2 — Glycosyl hydrolases family 16

Domain ID domain_id	d1macb_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.2 — Glycosyl hydrolases family 16

CATH v4.4 (2 domains)

Domain ID domain_id	1macA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	1macB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

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8. Citations (2)

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Unit-cell length a length_a	203.680 Å
Unit-cell length b length_b	42.410 Å
Unit-cell length c length_c	60.700 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.27 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1630
R_work r_work	—
R_free r_free	—

fit	/app/data/saxs_computation/ma/1mac/1mac.fit
pddf	/app/data/pr_computation/ma/1mac/1mac.pr.out
profile	/app/data/saxs_computation/ma/1mac/1mac.dat

CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE

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

1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution