SAXSdb — 3cox

▼

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

CHOLESTEROL OXIDASE

Brevibacterium sterolicum

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 46–552	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.80 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 3COX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1COY CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES Deposited 1993-06-14	Different ligand/ion	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 46–552（507 aa）	Not recorded	AND 3-BETA-HYDROXY-5-ANDROSTEN-17-ONE × 1 FAD FLAVIN-ADENINE DINUCLEOTIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å

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

View Construct and Data Evidence

UniProt name	CHOD_BREST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–507； UniProt 46–552

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3cox
Deposition date deposition_date	1993-06-14
Structure title title	CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES
Keywords keywords	OXIDOREDUCTASE(OXYGEN RECEPTOR); OXIDOREDUCTASE(OXYGEN RECEPTOR)
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	22.87 Å
Radius of gyration Rg (electron density) rg_electron	21.83 Å
Forward intensity I(0) i0	48258300.00
Molecular weight molecular_weight	53766.0 kDa
Excluded volume excluded_volume	67040 Å³
Envelope volume envelope_volume	75243 Å³
Hydration-shell volume shell_volume	27888 Å³
Envelope diameter envelope_diameter	77.2 Å
Shell Rg shell_rg	29.57 Å
Envelope Rg envelope_rg	22.00 Å
Shape Rg shape_rg	21.83 Å
Total Rg total_rg	22.70 Å
Total atoms total_atoms	3791
Residues n_residues	500
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	75.5 Å
Rg (real space) rg_real	22.76 Å
Rg uncertainty (real space) rg_real_error	0.37 Å
I(0) (real space) i0_real	4.8260e+07
I(0) uncertainty (real space) i0_real_error	6.1970e+05
Rg (reciprocal space) rg_reciprocal	22.79 Å
I(0) (reciprocal space) i0_reciprocal	48260000.0000
Solution quality estimate total_estimate	0.7182
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	74.4 Å
Skewness Skewness skewness	0.237
Kurtosis Kurtosis kurtosis	-0.305
Angular range angular_range	— – 0.3450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12560000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 0.307; Positv: 1.000; Valcen: 0.997; Smooth: 0.994

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	CHOLESTEROL OXIDASE
Molecular weight formula_weight	54891.7 kDa
EC 编号 ec_number	1.1.3.6
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	4244

APSRTLADGDRVPALVIGSGYGGAVAALRLTQAGIPTQIVEMGRSWDTPGSDGKIFCGMLNPDKRSMWLADKTDQPVSNFMGFGINKSIDRYVGVLDSERFSGIKVYQGRGVGGGSLVNGGMAVTPKRNYFEEILPSVDSNEMYNKYFPRANTGLGVNNIDQAWFESTEWYKFARTGRKTAQRSGFTTAFVPNVYDFEYMKKEAAGQVTKSGLGGEVIYGNNAGKKSLDKTYLAQAAATGKLTITTLHRVTKVAPATGSGYSVTMEQIDEQGNVVATKVVTADRVFFAAGSVGTSKLLVSMKAQGHLPNLSSQVGEGWGNNGNIMVGRANHMWDATGSKQATIPTMGIDNWADPTAPIFAEIAPLPAGLETYVSLYLAITKNPERARFQFNSGTGKVDLTWAQSQNQKGIDMAKKVFDKINQKEGTIYRTDLFGVYYKTWGDDFTYHPLGGVLLNKATDNFGRLPEYPGLYVVDGSLVPGNVGVNPFVTITALAERNMDKIISSDIQ

来源 Source

来源生物 organism	Brevibacterium sterolicum
NCBI Class编号 ncbi_taxonomy_id	1702

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	453

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3coxa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.2 — FAD-linked reductases, N-terminal domain

Domain ID domain_id	d3coxa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
Family Family family	d.16.1.1 — GMC oxidoreductases

CATH v4.4 (2 domains)

Domain ID domain_id	3coxA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	3coxA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	410 — Cholesterol Oxidase; domain 2
Homologous superfamily homologous superfamily	10 — Cholesterol Oxidase; domain 2

▶

8. Citations (3)

▶

Unit-cell length a length_a	67.720 Å
Unit-cell length b length_b	84.580 Å
Unit-cell length c length_c	88.130 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	1.800 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1560
R_work r_work	0.1560
R_free r_free	—

fit	/app/data/saxs_computation/co/3cox/3cox.fit
pddf	/app/data/pr_computation/co/3cox/3cox.pr.out
profile	/app/data/saxs_computation/co/3cox/3cox.dat

CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES

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

CHOLESTEROL OXIDASE

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