1pwc

penicilloyl acyl enzyme complex of the Streptomyces R61 DD-peptidase with penicillin G

Method: X-RAY DIFFRACTION Dmax: 59.8 Å Quality: REASONABLE

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

D-alanyl-D-alanine carboxypeptidase

OrganismNot specified

UniProt P15555

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 32–380 Fragment:DD-PEPTIDASE PNM OPEN FORM - PENICILLIN G × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;298 K;20% PEG 8000, 50mM Sodium Phosphate, pH 6.80, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.10 Å R-free 0.148

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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DAC_STRSR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–349; UniProt 32–380

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 1pwc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pwc
Deposition date deposition_date2003-07-01
Structure title titlepenicilloyl acyl enzyme complex of the Streptomyces R61 DD-peptidase with penicillin G
Keywords keywordsBETA-LACTAM, ANTIBIOTICS, PENICILLIN BINDING PROTEIN, ENZYME, PEPTIDOGLYCAN, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.93
Radius of gyration Rg (electron density) rg_electron18.76
Forward intensity I(0) i024693200.00
Molecular weight molecular_weight37316.0 kDa
Excluded volume excluded_volume46291 ų
Envelope volume envelope_volume50388 ų
Hydration-shell volume shell_volume21768 ų
Envelope diameter envelope_diameter61.3
Shell Rg shell_rg25.80
Envelope Rg envelope_rg18.99
Shape Rg shape_rg18.74
Total Rg total_rg19.67
Total atoms total_atoms2625
Residues n_residues345
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 dmax59.8
Rg (real space) rg_real19.77
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real2.4690e+07
I(0) uncertainty (real space) i0_real_error2.8060e+05
Rg (reciprocal space) rg_reciprocal19.80
I(0) (reciprocal space) i0_reciprocal24690000.0000
Solution quality estimate total_estimate0.7233
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5395000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 0.210; Positv: 1.000; Valcen: 0.983; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pwca_
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 (1 domains)

Domain ID domain_id1pwcA00
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 (4)

9. Files and Curves (10)