SAXSdb — 1utr

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

UTEROGLOBIN

Rattus norvegicus

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–96 Chain B； UniProt 1–96	Not recorded	PCB 4,4'-BIS([H]METHYLSULFONYL)-2,2',5,5'-TETRACHLOROBIPHENYL × 1	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	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 1UTR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CCD REFINED STRUCTURE OF RAT CLARA CELL 17 KDA PROTEIN AT 3.0 ANGSTROMS RESOLUTION Deposited 1991-09-17	Different construct Different mutation/modification Different ligand/ion Different experimental method Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 20–96（77 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UTER_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–96； UniProt 1–96 Author chain B； PDBConstruct 1–96； UniProt 1–96

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	1utr
Deposition date deposition_date	1995-09-01
Structure title title	UTEROGLOBIN-PCB COMPLEX (REDUCED FORM)
Keywords keywords	;UTEROGLOBIN, CLARA CELL 17 KDA PROTEIN (CC10), PHOSPHOLIPASE A2 INHIBITOR, CLARA CELL PHOSPHOLIPID-BINDING PROTEIN, PROGESTERONE BINDING, MAMMALIAN PCB-BINDING PROTEIN ;; MAMMALIAN PCB-BINDING PROTEIN
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	15.40 Å
Radius of gyration Rg (electron density) rg_electron	13.91 Å
Forward intensity I(0) i0	4344280.00
Molecular weight molecular_weight	15289.0 kDa
Excluded volume excluded_volume	19389 Å³
Envelope volume envelope_volume	21151 Å³
Hydration-shell volume shell_volume	12752 Å³
Envelope diameter envelope_diameter	46.1 Å
Shell Rg shell_rg	19.83 Å
Envelope Rg envelope_rg	14.26 Å
Shape Rg shape_rg	13.90 Å
Total Rg total_rg	15.18 Å
Total atoms total_atoms	2048
Residues n_residues	136
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	47.0 Å
Rg (real space) rg_real	15.38 Å
Rg uncertainty (real space) rg_real_error	0.08 Å
I(0) (real space) i0_real	4.2400e+06
I(0) uncertainty (real space) i0_real_error	3.4680e+04
Rg (reciprocal space) rg_reciprocal	15.30 Å
I(0) (reciprocal space) i0_reciprocal	4344000.0000
Solution quality estimate total_estimate	0.7314
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	21.4 Å
Skewness Skewness skewness	0.100
Kurtosis Kurtosis kurtosis	-0.412
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	9.7060
Highest regularization parameter α highest_alpha	1191000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.921; Stabil: 0.937; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.954

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1utra_
Class class	a — All alpha proteins
Fold Fold fold	a.101 — Uteroglobin-like
Superfamily Superfamily superfamily	a.101.1 — Uteroglobin-like
Family Family family	a.101.1.1 — Uteroglobin-like

Domain ID domain_id	d1utrb_
Class class	a — All alpha proteins
Fold Fold fold	a.101 — Uteroglobin-like
Superfamily Superfamily superfamily	a.101.1 — Uteroglobin-like
Family Family family	a.101.1.1 — Uteroglobin-like

CATH v4.4 (2 domains)

Domain ID domain_id	1utrA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	210 — Uteroglobin
Homologous superfamily homologous superfamily	10 — Secretoglobin

Domain ID domain_id	1utrB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	210 — Uteroglobin
Homologous superfamily homologous superfamily	10 — Secretoglobin

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8. Citations (4)

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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	UTEROGLOBIN
Molecular weight formula_weight	10457.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2048

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

UTEROGLOBIN-PCB COMPLEX (REDUCED FORM)

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

UTEROGLOBIN

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	4,4'-BIS([H]METHYLSULFONYL)-2,2',5,5'-TETRACHLOROBIPHENYL
Molecular weight formula_weight	448.2 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/ut/1utr/1utr.fit
pddf	/app/data/pr_computation/ut/1utr/1utr.pr.out
profile	/app/data/saxs_computation/ut/1utr/1utr.dat