5h75

Crystal structure of the MrsD-Protein A fusion protein

Method: X-RAY DIFFRACTION Dmax: 121.0 Å Quality: GOOD

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

Mersacidin decarboxylase,Immunoglobulin G-binding protein A

Staphylococcus aureus

UniProt P38507

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 223–269 Chain B; UniProt 223–269 Chain C; UniProt 223–269 Chain D; UniProt 223–269 Fragment:UNP RESIDUES 1-184,223-269 Mutation:K182Q,G240A FAD FLAVIN-ADENINE DINUCLEOTIDE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;277 K;0.94M sodium citrate pH 5.5 Resolution 2.74 Å R-free 0.243

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.

66 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 192–238; UniProt 223–269 Author chain B; PDBConstruct 192–238; UniProt 223–269 Author chain C; PDBConstruct 192–238; UniProt 223–269 Author chain D; PDBConstruct 192–238; UniProt 223–269

Mersacidin decarboxylase,Immunoglobulin G-binding protein A

Staphylococcus aureus

UniProt Q9RC23

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–184 Chain B; UniProt 1–184 Chain C; UniProt 1–184 Chain D; UniProt 1–184 Fragment:UNP RESIDUES 1-184,223-269 Mutation:K182Q,G240A FAD FLAVIN-ADENINE DINUCLEOTIDE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;277 K;0.94M sodium citrate pH 5.5 Resolution 2.74 Å R-free 0.243

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MRSD_BACSY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–191; UniProt 1–184 Author chain B; PDBConstruct 8–191; UniProt 1–184 Author chain C; PDBConstruct 8–191; UniProt 1–184 Author chain D; PDBConstruct 8–191; UniProt 1–184

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 5h75

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h75
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h75
Deposition date deposition_date2016-11-17
Structure title titleCrystal structure of the MrsD-Protein A fusion protein
Keywords keywordssynthetic protein, LYASE; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.24
Radius of gyration Rg (electron density) rg_electron32.79
Forward intensity I(0) i0143922000.00
Molecular weight molecular_weight96675.0 kDa
Excluded volume excluded_volume121410 ų
Envelope volume envelope_volume155730 ų
Hydration-shell volume shell_volume40401 ų
Envelope diameter envelope_diameter127.1
Shell Rg shell_rg38.66
Envelope Rg envelope_rg33.11
Shape Rg shape_rg32.83
Total Rg total_rg33.16
Total atoms total_atoms6800
Residues n_residues839
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 dmax121.0
Rg (real space) rg_real33.34
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real1.4390e+08
I(0) uncertainty (real space) i0_real_error2.3620e+06
Rg (reciprocal space) rg_reciprocal33.30
I(0) (reciprocal space) i0_reciprocal143900000.0000
Solution quality estimate total_estimate0.8162
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary30.2
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.067
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36520000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.655; Stabil: 0.973; Sysdev: 1.000; Positv: 1.000; Valcen: 0.890; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)