SAXSdb — 1qld

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

XYLANASE

PSEUDOMONAS FLUORESCENS

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 180–228	Fragment：CELLULOSE BINDING DOMAIN	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4.5；323 K；Ionic strength (raw mmCIF value) 100 MM NACL；Pressure AMBIENT NMR sample composition：90% WATER / 10% D2O	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 1QLD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CLX CATALYTIC CORE OF XYLANASE A Deposited 1995-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 265–611（347 aa） Fragment：CATALYTIC CORE, RESIDUES 264 - 611 Chain B 265–611（347 aa） Fragment：CATALYTIC CORE, RESIDUES 264 - 611	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 1.80 Å
1CLX CATALYTIC CORE OF XYLANASE A Deposited 1995-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 265–611（347 aa） Fragment：CATALYTIC CORE, RESIDUES 264 - 611 Chain D 265–611（347 aa） Fragment：CATALYTIC CORE, RESIDUES 264 - 611	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 1.80 Å
1E5N E246C mutant of P fluorescens subsp. cellulosa xylanase A in complex with xylopentaose Deposited 2000-07-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 264–611（348 aa） Fragment：CATALYTIC DOMAIN RESIDUES 264-611	Mutation：YES	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；HANGING DROP (10 MG/ML OF PROTEIN) WITH A RESERVOIR OF 0.1 M SODIUM CACODYLATE PH 6.5, 200 MM CALCIUM ACETATE, 1 MM BETA-MERCAPTOETHANOL, 14-18% PEG 8000	Resolution 3.20 Å R-free 0.245
1E5N E246C mutant of P fluorescens subsp. cellulosa xylanase A in complex with xylopentaose Deposited 2000-07-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 264–611（348 aa） Fragment：CATALYTIC DOMAIN RESIDUES 264-611	Mutation：YES	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；HANGING DROP (10 MG/ML OF PROTEIN) WITH A RESERVOIR OF 0.1 M SODIUM CACODYLATE PH 6.5, 200 MM CALCIUM ACETATE, 1 MM BETA-MERCAPTOETHANOL, 14-18% PEG 8000	Resolution 3.20 Å R-free 0.245
1E8R SOLUTION STRUCTURE OF TYPE X CBD Deposited 2000-09-28	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 179–228（50 aa） Fragment：TYPE X CELLULOSE BINDING DOMAIN (CBDX)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；323 K；Ionic strength (raw mmCIF value) 100MM NACL；Pressure AMBIENT NMR sample composition 1MM CBDX NMR sample composition 50MM SODIUM PHOSPHATE BUFFER NMR sample composition 100MM SODIUM CHLORIDE	Resolution not provided
1W2P The 3-dimensional structure of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-07	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 265–609（345 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611 Chain A 610–611（2 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.45 Å R-free 0.152
1W2P The 3-dimensional structure of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-07	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 265–609（345 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611 Chain B 610–611（2 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Not recorded	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.45 Å R-free 0.152
1W2V The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-09	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 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.55 Å R-free 0.186
1W2V The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-09	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.55 Å R-free 0.186
1W32 The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-12	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 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.20 Å R-free 0.144
1W32 The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-12	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 7	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.20 Å R-free 0.144
1W3H The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-15	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 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.251
1W3H The 3-dimensional structure of a thermostable mutant of a xylanase (Xyn10A) from Cellvibrio japonicus Deposited 2004-07-15	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 265–611（347 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 265-611	Mutation：YES	CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.251
1XYS CATALYTIC CORE OF XYLANASE A E246C MUTANT Deposited 1994-09-02	Different construct 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 265–611（347 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1XYS CATALYTIC CORE OF XYLANASE A E246C MUTANT Deposited 1994-09-02	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 265–611（347 aa）	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	XYNA_PSEFL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–50； UniProt 180–228

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	1qld
Deposition date deposition_date	1999-08-26
Structure title title	Solution structure of type X CBM
Keywords keywords	XYLANASE, BETA STRANDS, ANTI PARALLEL BETA SHEETS, XYLAN DEGRADATION, HYDROLASE, GLYCOSIDASE; XYLANASE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	11.08 Å
Radius of gyration Rg (electron density) rg_electron	9.81 Å
Forward intensity I(0) i0	796692.00
Molecular weight molecular_weight	5398.0 kDa
Excluded volume excluded_volume	6566 Å³
Envelope volume envelope_volume	6959 Å³
Hydration-shell volume shell_volume	6393 Å³
Envelope diameter envelope_diameter	34.8 Å
Shell Rg shell_rg	14.91 Å
Envelope Rg envelope_rg	10.49 Å
Shape Rg shape_rg	9.79 Å
Total Rg total_rg	11.31 Å
Total atoms total_atoms	721
Residues n_residues	50
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	36.8 Å
Rg (real space) rg_real	11.05 Å
Rg uncertainty (real space) rg_real_error	0.22 Å
I(0) (real space) i0_real	7.9670e+05
I(0) uncertainty (real space) i0_real_error	7.3570e+03
Rg (reciprocal space) rg_reciprocal	11.05 Å
I(0) (reciprocal space) i0_reciprocal	796700.0000
Solution quality estimate total_estimate	0.8919
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	13.5 Å
Skewness Skewness skewness	0.232
Kurtosis Kurtosis kurtosis	-0.346
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	93580.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.969

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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_id	d1qlda1
Class class	g — Small proteins
Fold Fold fold	g.29 — Type X cellulose binding domain, CBDX
Superfamily Superfamily superfamily	g.29.1 — Type X cellulose binding domain, CBDX
Family Family family	g.29.1.1 — Type X cellulose binding domain, CBDX

Domain ID domain_id	d1qlda2
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	1qldA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	32 — Xylanase; Chain A
Homologous superfamily homologous superfamily	30 — CBM10

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	XYLANASE
Molecular weight formula_weight	5400.0 kDa
EC 编号 ec_number	3.2.1.8
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	721

来源生物 organism	PSEUDOMONAS FLUORESCENS
NCBI Class编号 ncbi_taxonomy_id	294
宿主生物 host_organism	ESCHERICHIA COLI BL21

Solution structure of type X CBM

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

XYLANASE

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ql/1qld/1qld.fit
pddf	/app/data/pr_computation/ql/1qld/1qld.pr.out
profile	/app/data/saxs_computation/ql/1qld/1qld.dat