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1cle

STRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE

Method: X-RAY DIFFRACTION Dmax: 98.8 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CHOLESTEROL ESTERASE

OrganismNot specified

UniProt P32947

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 16–549 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PO4 PHOSPHATE ION × 1 CLL CHOLESTERYL LINOLEATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å
2 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 16–549 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PO4 PHOSPHATE ION × 1 CLL CHOLESTERYL LINOLEATE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name LIP3_CANRU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–534； UniProt 16–549 Author chain B； PDBConstruct 1–534； UniProt 16–549

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 1cle

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cle
Deposition date deposition_date1995-02-08
Structure title titleSTRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE
Keywords keywordsESTERASE, SUBSTRATE/PRODUCT-BOUND, LIPASE; LIPASE
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_guinier32.92 Å
Radius of gyration Rg (electron density) rg_electron31.69 Å
Forward intensity I(0) i0207307000.00
Molecular weight molecular_weight117270.0 kDa
Excluded volume excluded_volume147430 ų
Envelope volume envelope_volume176370 ų
Hydration-shell volume shell_volume45633 ų
Envelope diameter envelope_diameter98.8 Å
Shell Rg shell_rg39.69 Å
Envelope Rg envelope_rg31.07 Å
Shape Rg shape_rg31.67 Å
Total Rg total_rg32.37 Å
Total atoms total_atoms8260
Residues n_residues1068
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 dmax98.8 Å
Rg (real space) rg_real32.78 Å
Rg uncertainty (real space) rg_real_error0.57 Å
I(0) (real space) i0_real2.0730e+08
I(0) uncertainty (real space) i0_real_error2.7830e+06
Rg (reciprocal space) rg_reciprocal32.84 Å
I(0) (reciprocal space) i0_reciprocal207300000.0000
Solution quality estimate total_estimate0.9137
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.1 Å
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.701
Angular range angular_range— – 0.2400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34840000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.931
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1clea_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.17 — Fungal lipases
Domain ID domain_idd1cleb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.17 — Fungal lipases

CATH v4.4 (2 domains)

Domain ID domain_id1cleA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id1cleB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
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8. Citations (3)

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9. Files and Curves (10)