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5ovm

Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa

Method: SOLUTION NMR Dmax: 49.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Lipase chaperone

Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

UniProt Q01725

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 66–146 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.4；303 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition：450 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 5OVM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6GSF Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa Deposited 2018-06-14 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 66–146（81 aa）
Mutation：Y42A No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；303 K；Ionic strength (raw mmCIF value) 20；Pressure 1
NMR sample composition 530 uM [U-13C; U-15N] Lipase-interaction domain 1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

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

View Construct and Data Evidence
UniProt name LIFO_PSEAE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 9–89； UniProt 66–146

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 5ovm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5ovm
Deposition date deposition_date2017-08-29
Structure title titleSolution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa
Keywords keywordsLipase A, Lipase interaction domain 1, Chaperon, Pseudomonas aeruginosa, CHAPERONE; CHAPERONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.09 Å
Radius of gyration Rg (electron density) rg_electron13.63 Å
Forward intensity I(0) i0472661000.00
Molecular weight molecular_weight184010.0 kDa
Excluded volume excluded_volume230440 ų
Envelope volume envelope_volume31617 ų
Hydration-shell volume shell_volume16297 ų
Envelope diameter envelope_diameter57.4 Å
Shell Rg shell_rg22.56 Å
Envelope Rg envelope_rg16.43 Å
Shape Rg shape_rg13.61 Å
Total Rg total_rg13.92 Å
Total atoms total_atoms25820
Residues n_residues1640
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax49.9 Å
Rg (real space) rg_real14.01 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real4.7270e+08
I(0) uncertainty (real space) i0_real_error5.0260e+06
Rg (reciprocal space) rg_reciprocal14.02 Å
I(0) (reciprocal space) i0_reciprocal472700000.0000
Solution quality estimate total_estimate0.7693
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.7 Å
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha278600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.671; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)