5h7d

Crystal structure of the YgjG-protein A-Zpa963-calmodulin complex

Method: X-RAY DIFFRACTION Dmax: 260.9 Å Quality: GOOD

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

Putrescine aminotransferase,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 Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 220–267 Chain B; UniProt 220–267 Chain C; UniProt 220–267 Chain D; UniProt 220–267 Fragment:UNP RESIDUES 7-453,UNP RESIDUES 220-267 Mutation:N222V, G240A Zpa963,Calmodulin × 4 (O16305) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241
2 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 220–267 Chain J; UniProt 220–267 Chain M; UniProt 220–267 Chain N; UniProt 220–267 Fragment:UNP RESIDUES 7-453,UNP RESIDUES 220-267 Mutation:N222V, G240A Zpa963,Calmodulin × 4 (O16305) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241

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 126 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 452–499; UniProt 220–267 Author chain B; PDBConstruct 452–499; UniProt 220–267 Author chain C; PDBConstruct 452–499; UniProt 220–267 Author chain D; PDBConstruct 452–499; UniProt 220–267 Author chain I; PDBConstruct 452–499; UniProt 220–267 Author chain J; PDBConstruct 452–499; UniProt 220–267 Author chain M; PDBConstruct 452–499; UniProt 220–267 Author chain N; PDBConstruct 452–499; UniProt 220–267

Putrescine aminotransferase,Immunoglobulin G-binding protein A

Staphylococcus aureus

UniProt P42588

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 Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 7–453 Chain B; UniProt 7–453 Chain C; UniProt 7–453 Chain D; UniProt 7–453 Fragment:UNP RESIDUES 7-453,UNP RESIDUES 220-267 Mutation:N222V, G240A Zpa963,Calmodulin × 4 (O16305) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241
2 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 7–453 Chain J; UniProt 7–453 Chain M; UniProt 7–453 Chain N; UniProt 7–453 Fragment:UNP RESIDUES 7-453,UNP RESIDUES 220-267 Mutation:N222V, G240A Zpa963,Calmodulin × 4 (O16305) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAT_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–451; UniProt 7–453 Author chain B; PDBConstruct 5–451; UniProt 7–453 Author chain C; PDBConstruct 5–451; UniProt 7–453 Author chain D; PDBConstruct 5–451; UniProt 7–453 Author chain I; PDBConstruct 5–451; UniProt 7–453 Author chain J; PDBConstruct 5–451; UniProt 7–453 Author chain M; PDBConstruct 5–451; UniProt 7–453 Author chain N; PDBConstruct 5–451; UniProt 7–453

Zpa963,Calmodulin

Caenorhabditis elegans

UniProt O16305

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 Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 13–75 Chain F; UniProt 13–75 Chain G; UniProt 13–75 Chain H; UniProt 13–75 Fragment:RESIDUES 104-156,157-219 (UNP RESIDUES 13-75) Putrescine aminotransferase,Immunoglobulin G-binding protein A × 4 (P42588,P38507) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241
2 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain K; UniProt 13–75 Chain L; UniProt 13–75 Chain O; UniProt 13–75 Chain P; UniProt 13–75 Fragment:RESIDUES 104-156,157-219 (UNP RESIDUES 13-75) Putrescine aminotransferase,Immunoglobulin G-binding protein A × 4 (P42588,P38507) CA CALCIUM ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;296 K;0.1M HEPES pH 7.5, 20.7% PEG 300, 99mM calcium chloride Resolution 2.57 Å R-free 0.241

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_CAEEL
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 58–120; UniProt 13–75 Author chain F; PDBConstruct 58–120; UniProt 13–75 Author chain G; PDBConstruct 58–120; UniProt 13–75 Author chain H; PDBConstruct 58–120; UniProt 13–75 Author chain K; PDBConstruct 58–120; UniProt 13–75 Author chain L; PDBConstruct 58–120; UniProt 13–75 Author chain O; PDBConstruct 58–120; UniProt 13–75 Author chain P; PDBConstruct 58–120; UniProt 13–75

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 5h7d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h7d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h7d
Deposition date deposition_date2016-11-17
Structure title titleCrystal structure of the YgjG-protein A-Zpa963-calmodulin complex
Keywords keywordssynthetic protein, TRANSFERASE, IMMUNE SYSTEM-METAL BINDING PROTEIN complex; TRANSFERASE, IMMUNE SYSTEM/METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier71.69
Radius of gyration Rg (electron density) rg_electron71.46
Forward intensity I(0) i03861510000.00
Molecular weight molecular_weight528950.0 kDa
Excluded volume excluded_volume663400 ų
Envelope volume envelope_volume1052100 ų
Hydration-shell volume shell_volume122750 ų
Envelope diameter envelope_diameter256.5
Shell Rg shell_rg68.72
Envelope Rg envelope_rg70.85
Shape Rg shape_rg71.44
Total Rg total_rg71.51
Total atoms total_atoms37132
Residues n_residues4860
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 dmax260.9
Rg (real space) rg_real71.88
Rg uncertainty (real space) rg_real_error4.22
I(0) (real space) i0_real3.8620e+09
I(0) uncertainty (real space) i0_real_error9.8900e+07
Rg (reciprocal space) rg_reciprocal70.83
I(0) (reciprocal space) i0_reciprocal3853000000.0000
Solution quality estimate total_estimate0.8519
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.2
Skewness Skewness skewness0.358
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha131800000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.749; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.824

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)