1k0i

Pseudomonas aeruginosa phbh R220Q in complex with 100mM PHB

Method: X-RAY DIFFRACTION Dmax: 74.1 Å Quality: GOOD

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

P-HYDROXYBENZOATE HYDROXYLASE

Pseudomonas aeruginosa

UniProt P20586

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–394 Mutation:R220Q SO4 SULFATE ION × 16 SO3 SULFITE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;303 K;100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K Resolution 1.80 Å R-free 0.240
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–394 Mutation:R220Q SO4 SULFATE ION × 16 SO3 SULFITE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;303 K;100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K Resolution 1.80 Å R-free 0.240

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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHHY_PSEAE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–394; UniProt 1–394

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 1k0i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k0i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k0i
Deposition date deposition_date2001-09-19
Structure title titlePseudomonas aeruginosa phbh R220Q in complex with 100mM PHB
Keywords keywordsphbh, FAD, p-OHB, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.97
Radius of gyration Rg (electron density) rg_electron21.80
Forward intensity I(0) i038725400.00
Molecular weight molecular_weight46202.0 kDa
Excluded volume excluded_volume57055 ų
Envelope volume envelope_volume66974 ų
Hydration-shell volume shell_volume25417 ų
Envelope diameter envelope_diameter75.4
Shell Rg shell_rg28.89
Envelope Rg envelope_rg22.02
Shape Rg shape_rg21.78
Total Rg total_rg22.67
Total atoms total_atoms3240
Residues n_residues394
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 dmax74.1
Rg (real space) rg_real22.92
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.8730e+07
I(0) uncertainty (real space) i0_real_error4.6900e+05
Rg (reciprocal space) rg_reciprocal22.94
I(0) (reciprocal space) i0_reciprocal38730000.0000
Solution quality estimate total_estimate0.8910
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14120000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1k0ia1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1k0ia2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.2 — PHBH-like

CATH v4.4 (2 domains)

Domain ID domain_id1k0iA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1k0iA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology9 — D-Amino Acid Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — D-Amino Acid Oxidase, subunit A, domain 2

8. Citations (1)

9. Files and Curves (10)