1cbo

CHOLESTEROL OXIDASE FROM STREPTOMYCES HIS447ASN MUTANT

Method: X-RAY DIFFRACTION Dmax: 76.9 Å Quality: REASONABLE

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

PROTEIN (CHOLESTEROL OXIDASE)

Streptomyces sp.

UniProt P12676

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 43–546 Mutation:H447N FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.2;CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION USING THE HANGING DROP TECHNIQUE, PRECIPITANT CONDITIONS: 10-12% PEG 8000, 100MM SODIUM CACODYLATE PH 5.2, 75MM MNSO4 PROTEIN CONCENTRATION 8.5MG/ML Resolution 1.80 Å R-free 0.194

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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHOD_STRS0
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–504; UniProt 43–546

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1cbo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cbo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cbo
Deposition date deposition_date1999-02-26
Structure title titleCHOLESTEROL OXIDASE FROM STREPTOMYCES HIS447ASN MUTANT
Keywords keywordsFLAVOENZYME, STEROID METABOLISM, OXIDOREDUCTASE; FLAVOENZYME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.98
Radius of gyration Rg (electron density) rg_electron21.96
Forward intensity I(0) i051232000.00
Molecular weight molecular_weight54996.0 kDa
Excluded volume excluded_volume68425 ų
Envelope volume envelope_volume77675 ų
Hydration-shell volume shell_volume28545 ų
Envelope diameter envelope_diameter80.2
Shell Rg shell_rg29.79
Envelope Rg envelope_rg22.13
Shape Rg shape_rg21.96
Total Rg total_rg22.80
Total atoms total_atoms3876
Residues n_residues498
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax76.9
Rg (real space) rg_real22.85
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real5.1230e+07
I(0) uncertainty (real space) i0_real_error6.5020e+05
Rg (reciprocal space) rg_reciprocal22.88
I(0) (reciprocal space) i0_reciprocal51230000.0000
Solution quality estimate total_estimate0.7127
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.333
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13720000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 0.307; Positv: 1.000; Valcen: 0.998; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cboa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1cboa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.1 — GMC oxidoreductases

CATH v4.4 (2 domains)

Domain ID domain_id1cboA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1cboA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology410 — Cholesterol Oxidase; domain 2
Homologous superfamily homologous superfamily10 — Cholesterol Oxidase; domain 2

8. Citations (1)

9. Files and Curves (10)