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9xv5

Catalytic domain of N1484

Method: X-RAY DIFFRACTION Dmax: 52.5 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Lipase

Micromonospora ureilytica

UniProt A0A3N9XER1

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 54–312 Not recorded GLYCEROL × 1 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.40 Å R-free 0.177

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 9XV5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9XV8 Catalytic domain of N1484 E121S variant Deposited 2025-11-26 Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 54–312（259 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.64 Å R-free 0.225
9XV8 Catalytic domain of N1484 E121S variant Deposited 2025-11-26 Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 54–312（259 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.64 Å R-free 0.225

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A3N9XER1_9ACTN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–260； UniProt 54–312

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 9xv5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xv5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xv5
Deposition date deposition_date2025-11-25
最后修订 last_revision2026-06-03
Structure title titleCatalytic domain of N1484
Keywords keywordsPET hydrolase, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.83 Å
Radius of gyration Rg (electron density) rg_electron16.47 Å
Forward intensity I(0) i013500600.00
Molecular weight molecular_weight27445.0 kDa
Excluded volume excluded_volume34218 ų
Envelope volume envelope_volume36679 ų
Hydration-shell volume shell_volume18109 ų
Envelope diameter envelope_diameter51.5 Å
Shell Rg shell_rg23.13 Å
Envelope Rg envelope_rg16.67 Å
Shape Rg shape_rg16.47 Å
Total Rg total_rg17.43 Å
Total atoms total_atoms1932
Residues n_residues257
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 dmax52.5 Å
Rg (real space) rg_real17.66 Å
Rg uncertainty (real space) rg_real_error0.20 Å
I(0) (real space) i0_real1.3500e+07
I(0) uncertainty (real space) i0_real_error1.4070e+05
Rg (reciprocal space) rg_reciprocal17.68 Å
I(0) (reciprocal space) i0_reciprocal13500000.0000
Solution quality estimate total_estimate0.9043
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1 Å
Skewness Skewness skewness0.003
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.4450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4688000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.990
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)