SAXSdb — 1arb

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

ACHROMOBACTER PROTEASE I

Achromobacter lyticus

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 206–473	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.20 Å

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 1ARB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ARC THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE Deposited 1993-04-15	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 206–473（268 aa） Fragment：residues 206-473	Not recorded	TCK N-[(1S)-5-amino-1-(chloroacetyl)pentyl]-4-methylbenzenesulfonamide × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
4GPG X/N joint refinement of Achromobacter Lyticus Protease I free form at pD8.0 Deposited 2012-08-21	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 206–473（268 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared X-ray crystallization conditions VAPOR DIFFUSION；pH 8；297 K；20% w/v PEG 3350, 10mM Tris, HCl pH 8.0, 50% PEG 3350, HCl pD 8.0, VAPOR DIFFUSION, temperature 297K	Resolution not provided

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

View Construct and Data Evidence

UniProt name	API_ACHLY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–268； UniProt 206–473

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	1arb
Deposition date deposition_date	1993-04-15
Structure title title	THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE
Keywords keywords	HYDROLASE(SERINE PROTEASE); HYDROLASE(SERINE PROTEASE)
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	17.68 Å
Radius of gyration Rg (electron density) rg_electron	16.55 Å
Forward intensity I(0) i0	15207200.00
Molecular weight molecular_weight	27349.0 kDa
Excluded volume excluded_volume	33260 Å³
Envelope volume envelope_volume	35982 Å³
Hydration-shell volume shell_volume	17815 Å³
Envelope diameter envelope_diameter	55.4 Å
Shell Rg shell_rg	23.17 Å
Envelope Rg envelope_rg	16.74 Å
Shape Rg shape_rg	16.52 Å
Total Rg total_rg	17.52 Å
Total atoms total_atoms	1924
Residues n_residues	263
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	54.3 Å
Rg (real space) rg_real	17.53 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	1.5210e+07
I(0) uncertainty (real space) i0_real_error	1.6840e+05
Rg (reciprocal space) rg_reciprocal	17.55 Å
I(0) (reciprocal space) i0_reciprocal	15210000.0000
Solution quality estimate total_estimate	0.8988
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.2 Å
Skewness Skewness skewness	0.067
Kurtosis Kurtosis kurtosis	-0.493
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2996000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.972

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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) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1arba_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id	1arbA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1arbA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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8. Citations (1)

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Unit-cell length a length_a	39.540 Å
Unit-cell length b length_b	40.360 Å
Unit-cell length c length_c	43.930 Å
Unit-cell angle α angle_alpha	114.80 °
Unit-cell angle β angle_beta	113.73 °
Unit-cell angle γ angle_gamma	74.00 °
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	—

Resolution resolution	1.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.1490
R_work r_work	—
R_free r_free	—

Description description	ACHROMOBACTER PROTEASE I
Molecular weight formula_weight	27759.2 kDa
EC 编号 ec_number	3.4.21.50
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2077

THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

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

ACHROMOBACTER PROTEASE I

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Achromobacter lyticus
NCBI Class编号 ncbi_taxonomy_id	224

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	153

fit	/app/data/saxs_computation/ar/1arb/1arb.fit
pddf	/app/data/pr_computation/ar/1arb/1arb.pr.out
profile	/app/data/saxs_computation/ar/1arb/1arb.dat