5x3f

Crystal structure of the YgjG-Protein A-Zpa963-PKA catalytic domain

Method: X-RAY DIFFRACTION Dmax: 131.2 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 220–269 Fragment:UNP RESIDUES 7-453,220-269 Mutation:N222V, G240A Zpa963,cAMP-dependent protein kinase catalytic subunit alpha × 4 (P05132) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;296 K;91mM MES pH 5.5, 2.33M Na formate Resolution 3.38 Å R-free 0.227

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 452–501; UniProt 220–269

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 Fragment:UNP RESIDUES 7-453,220-269 Mutation:N222V, G240A Zpa963,cAMP-dependent protein kinase catalytic subunit alpha × 4 (P05132) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;296 K;91mM MES pH 5.5, 2.33M Na formate Resolution 3.38 Å R-free 0.227

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 6 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

Zpa963,cAMP-dependent protein kinase catalytic subunit alpha

Mus musculus

UniProt P05132

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 B; UniProt 19–351 Fragment:residues 97-156,UNP RESIDUES 11-343 Non-standard monomer:Yes (specific site not provided by mmCIF) Putrescine aminotransferase,Immunoglobulin G-binding protein A × 4 (P42588,P38507) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.5;296 K;91mM MES pH 5.5, 2.33M Na formate Resolution 3.38 Å R-free 0.227

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.

84 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 61–393; UniProt 19–351

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 5x3f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5x3f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5x3f
Deposition date deposition_date2017-02-05
Structure title titleCrystal structure of the YgjG-Protein A-Zpa963-PKA catalytic domain
Keywords keywordssynthetic protein, LYASE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.70
Radius of gyration Rg (electron density) rg_electron39.04
Forward intensity I(0) i0127726000.00
Molecular weight molecular_weight93881.0 kDa
Excluded volume excluded_volume118590 ų
Envelope volume envelope_volume162640 ų
Hydration-shell volume shell_volume36696 ų
Envelope diameter envelope_diameter131.6
Shell Rg shell_rg42.15
Envelope Rg envelope_rg38.14
Shape Rg shape_rg39.02
Total Rg total_rg39.29
Total atoms total_atoms6616
Residues n_residues841
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 dmax131.2
Rg (real space) rg_real39.07
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real1.2770e+08
I(0) uncertainty (real space) i0_real_error2.1760e+06
Rg (reciprocal space) rg_reciprocal38.85
I(0) (reciprocal space) i0_reciprocal127700000.0000
Solution quality estimate total_estimate0.8399
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.0
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.611
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16480000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.750; Smooth: 0.794

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5x3fA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Domain ID domain_id5x3fA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id5x3fB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5x3fB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)