SAXSdb — 1bxd

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

PROTEIN (OSMOLARITY SENSOR PROTEIN (ENVZ))

Escherichia coli BL21(DE3)

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 290–450	Fragment：RESIDUES 290-450	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	SOLUTION NMR NMR measurement conditions：pH 7；298 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 1BXD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1JOY SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR. Deposited 1998-12-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 223–289（67 aa） Fragment：RESIDUES 223-289 Chain B 223–289（67 aa） Fragment：RESIDUES 223-289	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；298 K	Resolution not provided

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

View Construct and Data Evidence

UniProt name	ENVZ_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–161； UniProt 290–450

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	1bxd
Deposition date deposition_date	1998-10-02
Structure title title	NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ
Keywords keywords	HISTIDINE KINASE, OSMOSENSOR, HIS-ASP PHOSPHORELAY SYSTEM, SIGNAL TRANSDUCTION, TRANSFERASE; TRANSFERASE
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	18.36 Å
Radius of gyration Rg (electron density) rg_electron	17.80 Å
Forward intensity I(0) i0	2022440000.00
Molecular weight molecular_weight	358040.0 kDa
Excluded volume excluded_volume	439550 Å³
Envelope volume envelope_volume	90516 Å³
Hydration-shell volume shell_volume	29714 Å³
Envelope diameter envelope_diameter	83.6 Å
Shell Rg shell_rg	32.94 Å
Envelope Rg envelope_rg	26.06 Å
Shape Rg shape_rg	17.80 Å
Total Rg total_rg	18.14 Å
Total atoms total_atoms	49620
Residues n_residues	3220
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	48.6 Å
Rg (real space) rg_real	17.35 Å
Rg uncertainty (real space) rg_real_error	0.06 Å
I(0) (real space) i0_real	1.9220e+09
I(0) uncertainty (real space) i0_real_error	1.6880e+07
Rg (reciprocal space) rg_reciprocal	18.44 Å
I(0) (reciprocal space) i0_reciprocal	2022000000.0000
Solution quality estimate total_estimate	0.6848
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	19.7 Å
Skewness Skewness skewness	0.282
Kurtosis Kurtosis kurtosis	-0.418
Angular range angular_range	— – 0.4350 Å⁻¹
Current regularization parameter α current_alpha	4.0920
Highest regularization parameter α highest_alpha	1346000.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.004; Oscil: 0.988; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bxda_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamily	d.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family family	d.122.1.3 — Histidine kinase

CATH v4.4 (1 domains)

Domain ID domain_id	1bxdA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

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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	PROTEIN (OSMOLARITY SENSOR PROTEIN (ENVZ))
Molecular weight formula_weight	17417.7 kDa
EC 编号 ec_number	2.7.3.-
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	49620

来源生物 organism	Escherichia coli BL21(DE3)
NCBI Class编号 ncbi_taxonomy_id	469008
宿主生物 host_organism	Escherichia coli BL21(DE3)

NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ

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

PROTEIN (OSMOLARITY SENSOR PROTEIN (ENVZ))

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	506.2 kDa
Source method src_method	syn
Copy count entity_count	1

fit	/app/data/saxs_computation/bx/1bxd/1bxd.fit
pddf	/app/data/pr_computation/bx/1bxd/1bxd.pr.out
profile	/app/data/saxs_computation/bx/1bxd/1bxd.dat