9zpb

Crystal structure of Phosphoribosylaminoimidazole carboxylase from Burkholderia xenovorans (AMP complex)

Method: X-RAY DIFFRACTION Dmax: 119.3 Å Quality: GOOD

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

N5-carboxyaminoimidazole ribonucleotide synthase

Paraburkholderia xenovorans LB400

UniProt Q13UJ9

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 9–397 Fragment:S9-T397 AMP ADENOSINE MONOPHOSPHATE × 1 PGE TRIETHYLENE GLYCOL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291 K;BRK E6: 100 mM sodium citrate, pH 5.5, 200 mM sodium malonate, pH 5.0, 20% PEG 2000 MME. BuxeA.00036.a.B2.PW39468 at 23.8 mg/mL. Cocrystallization with 3mM AMP, plate 20558 E6 drop 3, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant Resolution 2.19 Å R-free 0.204
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 9–397 Fragment:S9-T397 AMP ADENOSINE MONOPHOSPHATE × 1 MG MAGNESIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291 K;BRK E6: 100 mM sodium citrate, pH 5.5, 200 mM sodium malonate, pH 5.0, 20% PEG 2000 MME. BuxeA.00036.a.B2.PW39468 at 23.8 mg/mL. Cocrystallization with 3mM AMP, plate 20558 E6 drop 3, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant Resolution 2.19 Å R-free 0.204
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 9–397 Fragment:S9-T397 AMP ADENOSINE MONOPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291 K;BRK E6: 100 mM sodium citrate, pH 5.5, 200 mM sodium malonate, pH 5.0, 20% PEG 2000 MME. BuxeA.00036.a.B2.PW39468 at 23.8 mg/mL. Cocrystallization with 3mM AMP, plate 20558 E6 drop 3, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant Resolution 2.19 Å R-free 0.204
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 9–397 Fragment:S9-T397 AMP ADENOSINE MONOPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;291 K;BRK E6: 100 mM sodium citrate, pH 5.5, 200 mM sodium malonate, pH 5.0, 20% PEG 2000 MME. BuxeA.00036.a.B2.PW39468 at 23.8 mg/mL. Cocrystallization with 3mM AMP, plate 20558 E6 drop 3, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant Resolution 2.19 Å R-free 0.204

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.

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

View Construct and Data Evidence
UniProt name Q13UJ9_PARXL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–397; UniProt 9–397 Author chain B; PDBConstruct 9–397; UniProt 9–397 Author chain C; PDBConstruct 9–397; UniProt 9–397 Author chain D; PDBConstruct 9–397; UniProt 9–397

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 9zpb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zpb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zpb
Deposition date deposition_date2025-12-16
最后修订 last_revision2025-12-24
Structure title titleCrystal structure of Phosphoribosylaminoimidazole carboxylase from Burkholderia xenovorans (AMP complex)
Keywords keywords;SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE, Phosphoribosylaminoimidazole carboxylase, LYASE ;; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.33
Radius of gyration Rg (electron density) rg_electron36.79
Forward intensity I(0) i0429829000.00
Molecular weight molecular_weight164840.0 kDa
Excluded volume excluded_volume204940 ų
Envelope volume envelope_volume256440 ų
Hydration-shell volume shell_volume57046 ų
Envelope diameter envelope_diameter127.0
Shell Rg shell_rg43.57
Envelope Rg envelope_rg36.83
Shape Rg shape_rg36.79
Total Rg total_rg37.16
Total atoms total_atoms11564
Residues n_residues1549
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 dmax119.3
Rg (real space) rg_real37.23
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real4.2980e+08
I(0) uncertainty (real space) i0_real_error6.8380e+06
Rg (reciprocal space) rg_reciprocal37.30
I(0) (reciprocal space) i0_reciprocal429900000.0000
Solution quality estimate total_estimate0.8965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70310000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)