1pio

AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS

Method: X-RAY DIFFRACTION Dmax: 77.6 Å Quality: GOOD

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

BETA-LACTAMASE

Staphylococcus aureus

UniProt P00807

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 25–281 Chain B; UniProt 25–281 Mutation:INS(MET 30), A238S, DEL(I239) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.80 Å R-free 0.189

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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLAC_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–257; UniProt 25–281 Author chain B; PDBConstruct 2–257; UniProt 25–281

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 1pio

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pio
Deposition date deposition_date1995-10-11
Structure title titleAN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS
Keywords keywordsHYDROLASE (ACTING ON CYCLIC AMIDES); HYDROLASE (ACTING ON CYCLIC AMIDES)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.09
Radius of gyration Rg (electron density) rg_electron23.34
Forward intensity I(0) i050379600.00
Molecular weight molecular_weight57424.0 kDa
Excluded volume excluded_volume73004 ų
Envelope volume envelope_volume82472 ų
Hydration-shell volume shell_volume28994 ų
Envelope diameter envelope_diameter80.3
Shell Rg shell_rg31.07
Envelope Rg envelope_rg23.48
Shape Rg shape_rg23.31
Total Rg total_rg24.31
Total atoms total_atoms4044
Residues n_residues512
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 dmax77.6
Rg (real space) rg_real24.03
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real5.0380e+07
I(0) uncertainty (real space) i0_real_error6.3700e+05
Rg (reciprocal space) rg_reciprocal24.05
I(0) (reciprocal space) i0_reciprocal50380000.0000
Solution quality estimate total_estimate0.8926
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19590000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1pioa_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase
Domain ID domain_idd1piob_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

CATH v4.4 (2 domains)

Domain ID domain_id1pioA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
Domain ID domain_id1pioB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily

8. Citations (3)

9. Files and Curves (10)