SAXSdb — 1v0a

▼

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

ENDOGLUCANASE H

CLOSTRIDIUM THERMOCELLUM

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 655–821	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；pH 6.00	Resolution 1.98 Å R-free 0.232

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 1V0A	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BV9 HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A Deposited 2005-06-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–304（279 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 26-304	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 0.3-1.2M NA FORMATE, 0.1M NA CACODYLATE BUFFERED AT PH 6.5 AND 5-20% PEG 4K	Resolution 1.50 Å R-free 0.157
2BVD HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A Deposited 2005-06-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–304（279 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 26-304	Not recorded	ISX (3R,4R,5R)-4-hydroxy-5-(hydroxymethyl)piperidin-3-yl beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CO-CRYSTALLIZED WITH THE LIGAND FROM 0.15 M AMMONIUM SULPHATE, 30% PEG 5K MME BUFFERED TO PH 6.5 WITH MES	Resolution 1.60 Å R-free 0.186
2CIP Structure of the Michaelis complex of a family 26 lichenase Deposited 2006-03-24	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 26–304（279 aa） Fragment：RESIDUES 26-304	Mutation：YES	ZZ1 4-METHYL-2H-CHROMEN-2-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.15 M AMMONIUM SULPHATE, 30 % PEG 5K MME BUFFERED TO PH6.5 WITH 0.1 M MES, pH 6.50	Resolution 1.40 Å R-free 0.179
2CIT Structure of the covalent intermediate of a family 26 lichenase Deposited 2006-03-24	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 26–304（279 aa） Fragment：RESIDUES 26-304	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.15 M AMMONIUM SULPHATE, 30 % PEG 5K MME BUFFERED TO PH 6.5 WITH 0.1 M MES	Resolution 1.40 Å R-free 0.179
2LRO Solution structure, dynamics and binding studies of CtCBM11 Deposited 2012-04-11	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 655–821（167 aa） Fragment：CBM11 domain residues 655-821	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 0.75；Pressure ambient NMR sample composition 1 mM [U-13C; U-15N] protein_1, 0.75 mM potassium phosphate, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2LRP Solution structure, dynamics and binding studies of CtCBM11 Deposited 2012-04-11	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 655–821（167 aa） Fragment：CBM11 domain residues 655-821	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7.5；323 K；Ionic strength (raw mmCIF value) 0.75；Pressure ambient NMR sample composition 1 mM [U-13C; U-15N] protein_1, 0.75 mM potassium phosphate, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2V3G Structure of a family 26 lichenase in complex with noeuromycin Deposited 2007-06-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 26–305（280 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 26-305	Not recorded	BGC beta-D-glucopyranose × 1 NOY (2R,3S,4R,5R)-5-(HYDROXYMETHYL)PIPERIDINE-2,3,4-TRIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；CO-CRYSTALLIZED WITH THE LIGAND FROM 0.15 M AMMONIUM SULPHATE, 30% PEG 5K MME BUFFERED TO PH 6.5 WITH MES AND SEEDED	Resolution 1.20 Å R-free 0.144
2VI0 Lichenase CtLic26 in complex with a thio-oligosaccharide Deposited 2007-11-26	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 26–304（279 aa） Fragment：RESIDUES 26-304	Mutation：G271E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；0.15 M AMMONIUM SULPHATE, 30 % PEG 5K, MME, 0.1 M MES PH 6.5	Resolution 1.51 Å R-free 0.189
4U3A Crystal structure of CtCel5E Deposited 2014-07-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.1 M sodium acetate and 21% (W/V) PEG 4000	Resolution 2.42 Å R-free 0.248
4U3A Crystal structure of CtCel5E Deposited 2014-07-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.1 M sodium acetate and 21% (W/V) PEG 4000	Resolution 2.42 Å R-free 0.248
4U5I Complex structure of mutant CtCel5E (E314A) with xylobiose Deposited 2014-07-25	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 290–654（365 aa） Fragment：UNP residues 290-654	Mutation：E314A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.2 M ammonium acetate, 0.1 M sodium acetate and 21% (W/V) PEG 4000	Resolution 2.50 Å R-free 0.252
4U5I Complex structure of mutant CtCel5E (E314A) with xylobiose Deposited 2014-07-25	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 290–654（365 aa） Fragment：UNP residues 290-654	Mutation：E314A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.2 M ammonium acetate, 0.1 M sodium acetate and 21% (W/V) PEG 4000	Resolution 2.50 Å R-free 0.252
4U5K Complex structure of mutant CtCel5E (E314A) with cellobiose Deposited 2014-07-25	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 290–654（365 aa） Fragment：UNP residues 290-654	Mutation：E314A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.2M ammonium acetate, 0.1M sodium acetate, 21% (W/V) PEG 4000	Resolution 2.65 Å R-free 0.255
4U5K Complex structure of mutant CtCel5E (E314A) with cellobiose Deposited 2014-07-25	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 290–654（365 aa） Fragment：UNP residues 290-654	Mutation：E314A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；0.2M ammonium acetate, 0.1M sodium acetate, 21% (W/V) PEG 4000	Resolution 2.65 Å R-free 0.255
5BYW Crystal structure of engineered trifunctional CtCEL5E Deposited 2015-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；50mM sodium acetate, 8% PEG 4000	Resolution 2.60 Å R-free 0.260
5BYW Crystal structure of engineered trifunctional CtCEL5E Deposited 2015-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；50mM sodium acetate, 8% PEG 4000	Resolution 2.60 Å R-free 0.260
5BYW Crystal structure of engineered trifunctional CtCEL5E Deposited 2015-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；50mM sodium acetate, 8% PEG 4000	Resolution 2.60 Å R-free 0.260
5BYW Crystal structure of engineered trifunctional CtCEL5E Deposited 2015-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；50mM sodium acetate, 8% PEG 4000	Resolution 2.60 Å R-free 0.260
5BYW Crystal structure of engineered trifunctional CtCEL5E Deposited 2015-06-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 290–654（365 aa） Fragment：UNP residues 290-654	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；298 K；50mM sodium acetate, 8% PEG 4000	Resolution 2.60 Å R-free 0.260
6R31 Family 11 Carbohydrate-Binding Module from Clostridium thermocellum in complex with beta-1,3-1,4-mixed-linked tetrasaccharide Deposited 2019-03-19	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 655–821（167 aa）	Not recorded	CA CALCIUM ION × 2 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293.15 K；20-28% (m/v) polyethyleneglycol (PEG) 3350, 0.2 M potassium phosphate, 0.1 M sodium acetate buffer pH 4.6	Resolution 2.60 Å R-free 0.254
6R3M Family 11 Carbohydrate-Binding Module from Clostridium thermocellum in complex with beta-1,3-1,4-mixed-linked tetrasaccharide Deposited 2019-03-20	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 655–821（167 aa）	Not recorded	CA CALCIUM ION × 2 ACT ACETATE ION × 1 PO4 PHOSPHATE ION × 4 GLC alpha-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293.15 K；20-28% (m/v) polyethyleneglycol (PEG) 3350, 0.2 M potassium phosphate, 0.1 M sodium acetate buffer pH 4.6	Resolution 1.45 Å R-free 0.208
6ZPL Inward-open structure of human glycine transporter 1 in complex with a benzoylisoindoline inhibitor, sybody Sb_GlyT1#7 and bound Na and Cl ions. Deposited 2020-07-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 31–303（273 aa）	Not recorded	QET [5-fluoranyl-6-(oxan-4-yloxy)-1,3-dihydroisoindol-2-yl]-[5-methylsulfonyl-2-[2,2,3,3,3-pentakis(fluoranyl)propoxy]phenyl]methanone × 2 NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 7；292.75 K；Crystals appeared in 3-10 days in 0.1 M ADA pH 7, 13-25% PEG600, 4-14% v/v, 1,3-Butanediol with the longest dimension of 2-5 um.	Resolution 3.94 Å R-free 0.291
8XVI Cryo-EM structure of ETAR bound with Endothelin1 Deposited 2024-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 26–304（279 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
8XVJ Cryo-EM structure of ETAR bound with Macitentan Deposited 2024-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 26–304（279 aa）	Not recorded	A1D5I Macitentan × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
8XVK Cryo-EM structure of ETAR bound with Ambrisentan Deposited 2024-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 26–304（279 aa）	Not recorded	A1D5J Ambrisentan × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.21 Å
8XVL Cryo-EM structure of ETAR bound with Zibotentan Deposited 2024-01-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 26–304（279 aa）	Not recorded	A1D5L Zibotentan × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.22 Å

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GUNH_CLOTM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–170； UniProt 655–821

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1v0a
Deposition date deposition_date	2004-03-25
Structure title title	Family 11 Carbohydrate-Binding Module of cellulosomal cellulase Lic26A-Cel5E of Clostridium thermocellum
Keywords keywords	CARBOHYDRATE BINDING MODULE, CELLULOSOME, CLOSTRIDIUM THERMOCELLUM, CELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	17.18 Å
Radius of gyration Rg (electron density) rg_electron	15.74 Å
Forward intensity I(0) i0	7499750.00
Molecular weight molecular_weight	19383.0 kDa
Excluded volume excluded_volume	23800 Å³
Envelope volume envelope_volume	26762 Å³
Hydration-shell volume shell_volume	14479 Å³
Envelope diameter envelope_diameter	59.6 Å
Shell Rg shell_rg	21.55 Å
Envelope Rg envelope_rg	16.19 Å
Shape Rg shape_rg	15.71 Å
Total Rg total_rg	16.81 Å
Total atoms total_atoms	1345
Residues n_residues	165
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

▼

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

Maximum dimension Dmax dmax	59.9 Å
Rg (real space) rg_real	17.11 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	7.5000e+06
I(0) uncertainty (real space) i0_real_error	9.9460e+04
Rg (reciprocal space) rg_reciprocal	17.12 Å
I(0) (reciprocal space) i0_reciprocal	7500000.0000
Solution quality estimate total_estimate	0.7879
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.3 Å
Skewness Skewness skewness	0.228
Kurtosis Kurtosis kurtosis	-0.234
Angular range angular_range	— – 0.4650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1013000.0000
Real-space data points n_real_points	77
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ENDOGLUCANASE H
Molecular weight formula_weight	20073.3 kDa
EC 编号 ec_number	3.2.1.4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1527

MASAVGEKMLDDFEGVLNWGSYSGEGAKVSTKIVSGKTGNGMEVSYTGTTDGYWGTVYSLPDGDWSKWLKISFDIKSVDGSANEIRFMIAEKSINGVGDGEHWVYSITPDSSWKTIEIPFSSFRRRLDYQPPGQDMSGTLDLDNIDSIHFMYANNKSGKFVVDNIKLIGALEHHHHHH

来源 Source

来源生物 organism	CLOSTRIDIUM THERMOCELLUM
NCBI Class编号 ncbi_taxonomy_id	1515
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 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	182

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1v0aa1
Class class	b — All beta proteins
Fold Fold fold	b.18 — Galactose-binding domain-like
Superfamily Superfamily superfamily	b.18.1 — Galactose-binding domain-like
Family Family family	b.18.1.30 — CBM11

Domain ID domain_id	d1v0aa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1v0aa3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	1v0aA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

▶

8. Citations (1)

▶

Unit-cell length a length_a	75.143 Å
Unit-cell length b length_b	50.892 Å
Unit-cell length c length_c	40.868 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.980 Å
Low-resolution limit resolution_low	19.000 Å
R factor r_factor	0.1950
R_work r_work	0.1930
R_free r_free	0.2320

fit	/app/data/saxs_computation/v0/1v0a/1v0a.fit
pddf	/app/data/pr_computation/v0/1v0a/1v0a.pr.out
profile	/app/data/saxs_computation/v0/1v0a/1v0a.dat

Family 11 Carbohydrate-Binding Module of cellulosomal cellulase Lic26A-Cel5E of Clostridium thermocellum

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

ENDOGLUCANASE H

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

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction