SAXSdb — 1is9

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

endoglucanase A

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 33–395	Fragment：residues 1-363	HG MERCURY (II) ION × 6 CL CHLORIDE ION × 7	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.03 Å R-free 0.149

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 1IS9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CEM ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395 Deposited 1995-12-04	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–395（363 aa） Fragment：CATALYTIC CORE RESIDUES 33-395	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.65 Å R-free 0.191
1KWF Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate Deposited 2002-01-29	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 33–395（363 aa） Fragment：catalytic core (residues 33-395)	Mutation：E95Q	BGC beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 0.94 Å R-free 0.113

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

View Construct and Data Evidence

UniProt name	GUNA_CLOTM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–363； UniProt 33–395

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	1is9
Deposition date deposition_date	2001-11-26
Structure title title	Endoglucanase A from Clostridium thermocellum at atomic resolution
Keywords keywords	endoglucanase family 8, Hg derivative, HYDROLASE; HYDROLASE
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	19.47 Å
Radius of gyration Rg (electron density) rg_electron	18.47 Å
Forward intensity I(0) i0	32321100.00
Molecular weight molecular_weight	41162.0 kDa
Excluded volume excluded_volume	49622 Å³
Envelope volume envelope_volume	53223 Å³
Hydration-shell volume shell_volume	22857 Å³
Envelope diameter envelope_diameter	58.1 Å
Shell Rg shell_rg	26.02 Å
Envelope Rg envelope_rg	18.77 Å
Shape Rg shape_rg	18.56 Å
Total Rg total_rg	19.06 Å
Total atoms total_atoms	2822
Residues n_residues	358
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	58.2 Å
Rg (real space) rg_real	19.29 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	3.2320e+07
I(0) uncertainty (real space) i0_real_error	3.3790e+05
Rg (reciprocal space) rg_reciprocal	19.32 Å
I(0) (reciprocal space) i0_reciprocal	32320000.0000
Solution quality estimate total_estimate	0.7548
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.2 Å
Skewness Skewness skewness	0.028
Kurtosis Kurtosis kurtosis	-0.516
Angular range angular_range	— – 0.4100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5674000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 0.356; Positv: 1.000; Valcen: 0.975; Smooth: 0.997

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	endoglucanase A
Molecular weight formula_weight	40345.3 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	3600

AGVPFNTKYPYGPTSIADNQSEVTAMLKAEWEDWKSKRITSNGAGGYKRVQRDASTNYDTVSEGMGYGLLLAVCFNEQALFDDLYRYVKSHFNGNGLMHWHIDANNNVTSHDGGDGAATDADEDIALALIFADKQWGSSGAINYGQEARTLINNLYNHCVEHGSYVLKPGDRWGGSSVTNPSYFAPAWYKVYAQYTGDTRWNQVADKCYQIVEEVKKYNNGTGLVPDWCTASGTPASGQSYDYKYDATRYGWRTAVDYSWFGDQRAKANCDMLTKFFARDGAKGIVDGYTIQGSKISNNHNASFIGPVAAASMTGYDLNFAKELYRETVAVKDSEYYGYYGNSLRLLTLLYITGNFPNPLSDL

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	MERCURY (II) ION
Molecular weight formula_weight	200.6 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	760

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1is9a_
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.1 — Six-hairpin glycosidases
Family Family family	a.102.1.2 — Cellulases catalytic domain

CATH v4.4 (1 domains)

Domain ID domain_id	1is9A00
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	49.441 Å
Unit-cell length b length_b	62.829 Å
Unit-cell length c length_c	103.891 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 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.030 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	—
R_work r_work	0.1310
R_free r_free	0.1490

fit	/app/data/saxs_computation/is/1is9/1is9.fit
pddf	/app/data/pr_computation/is/1is9/1is9.pr.out
profile	/app/data/saxs_computation/is/1is9/1is9.dat

Endoglucanase A from Clostridium thermocellum at atomic resolution

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

endoglucanase A

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