SAXSdb — 1ulp

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

ENDOGLUCANASE C

Cellulomonas fimi

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 33–184	Fragment：N-TERMINAL CELLULOSE-BINDING DOMAIN	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.9；308 K	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 1ULP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CX1 SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES Deposited 1999-08-27	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–328（153 aa） Fragment：RESIDUES 176-328	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；35 K；Ionic strength (raw mmCIF value) 50mMNACL；Pressure 1 NMR sample composition 1.5 TO 2 MM CBDN2 U-15N, 13C; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5, NMR sample composition 1.5 TO 2 MM CBDN2 U-15N; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5, NMR sample composition 1.5 TO 2 MM CBDN2 UNLABELED; UP TO 22-FOLD MOLAR EXCESS OF CELLOPENTAOSE; IN 50 MM NACL, 50 MM PHOSPHATE BUFFER K AT PH* 6.5,	Resolution not provided
1GU3 CBM4 structure and function Deposited 2002-01-22	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 33–181（149 aa） Fragment：CARBOHYDRATE BINDING MODULE FAMILY 4, RESIDUES 1-149	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；1.8M AMMONIUM SULFATE, 3% ISOPROPANOL, pH 5.00	Resolution 2.30 Å R-free 0.257
1ULO N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-07-27	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–184（152 aa） Fragment：N-TERMINAL CELLULOSE-BINDING DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.9；308 K	Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GUNC_CELFI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–152； UniProt 33–184

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	1ulp
Deposition date deposition_date	1996-07-27
Structure title title	N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 25 STRUCTURES
Keywords keywords	CELLULOSE DEGRADATION, CELLULOSE-BINDING DOMAIN, HYDROLASE; CELLULOSE DEGRADATION
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	15.51 Å
Radius of gyration Rg (electron density) rg_electron	14.98 Å
Forward intensity I(0) i0	2156200000.00
Molecular weight molecular_weight	385220.0 kDa
Excluded volume excluded_volume	476340 Å³
Envelope volume envelope_volume	34147 Å³
Hydration-shell volume shell_volume	16688 Å³
Envelope diameter envelope_diameter	58.0 Å
Shell Rg shell_rg	23.36 Å
Envelope Rg envelope_rg	17.74 Å
Shape Rg shape_rg	14.97 Å
Total Rg total_rg	15.11 Å
Total atoms total_atoms	52625
Residues n_residues	3800
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	51.5 Å
Rg (real space) rg_real	15.44 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	2.1560e+09
I(0) uncertainty (real space) i0_real_error	2.3270e+07
Rg (reciprocal space) rg_reciprocal	15.45 Å
I(0) (reciprocal space) i0_reciprocal	2156000000.0000
Solution quality estimate total_estimate	0.8895
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.9 Å
Skewness Skewness skewness	0.139
Kurtosis Kurtosis kurtosis	-0.430
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	300100.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.993

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ulpa_
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.18.1.14 — CBM4/9

CATH v4.4 (1 domains)

Domain ID domain_id	1ulpA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	260 — Galactose-binding domain-like

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8. Citations (3)

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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	ENDOGLUCANASE C
Molecular weight formula_weight	15429.7 kDa
EC 编号 ec_number	3.2.1.4
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	52625

来源生物 organism	Cellulomonas fimi
NCBI Class编号 ncbi_taxonomy_id	1708
宿主生物 host_organism	Escherichia coli

N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 25 STRUCTURES

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

ENDOGLUCANASE C

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (3)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ul/1ulp/1ulp.fit
pddf	/app/data/pr_computation/ul/1ulp/1ulp.pr.out
profile	/app/data/saxs_computation/ul/1ulp/1ulp.dat