1b90

BACILLUS CEREUS BETA-AMYLASE APO FORM

Method: X-RAY DIFFRACTION Dmax: 82.2 Å Quality: EXCELLENT

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

PROTEIN (BETA-AMYLASE)

Bacillus cereus

UniProt P36924

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 31–546 Not recorded ACT ACETATE ION × 1 SO4 SULFATE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;HANGING DROP VAPOR DIFFUSION AGAINST 0.1 M ACETATE BUFFER PH 4.6, 18% PEG 6000 AND 5% SATN. AMMONIUM SULFATE WITH A PROTEIN CONCENTRATION OF 10MG/ML. Resolution 2.50 Å R-free 0.247

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.

12 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMYB_BACCE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–516; UniProt 31–546

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 1b90

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b90
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b90
Deposition date deposition_date1999-03-06
Structure title titleBACILLUS CEREUS BETA-AMYLASE APO FORM
Keywords keywordsHYDROLASE(O-GLYCOSYL), HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.30
Radius of gyration Rg (electron density) rg_electron25.49
Forward intensity I(0) i054531300.00
Molecular weight molecular_weight58491.0 kDa
Excluded volume excluded_volume73394 ų
Envelope volume envelope_volume86422 ų
Hydration-shell volume shell_volume28862 ų
Envelope diameter envelope_diameter87.6
Shell Rg shell_rg32.13
Envelope Rg envelope_rg25.73
Shape Rg shape_rg25.47
Total Rg total_rg26.23
Total atoms total_atoms4129
Residues n_residues516
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 dmax82.2
Rg (real space) rg_real26.30
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real5.4530e+07
I(0) uncertainty (real space) i0_real_error7.1600e+05
Rg (reciprocal space) rg_reciprocal26.30
I(0) (reciprocal space) i0_reciprocal54530000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11120000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.900

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1b90a1
Class classb — All beta proteins
Fold Fold foldb.3 — Prealbumin-like
Superfamily Superfamily superfamilyb.3.1 — Starch-binding domain-like
Family Family familyb.3.1.1 — Starch-binding domain
Domain ID domain_idd1b90a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.8 — (Trans)glycosidases
Family Family familyc.1.8.1 — Amylase, catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id1b90A01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily80 — Glycosidases
Domain ID domain_id1b90A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)