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1ci8

ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI: AN ESTERASE WITH (BETA)-LACTAMASE FOLD.

Method: X-RAY DIFFRACTION Dmax: 100.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (CARBOXYLESTERASE)

Burkholderia gladioli

UniProt Q9KX40

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 1–392 Chain B； UniProt 1–392 Not recorded IPA ISOPROPYL ALCOHOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；10% PEG 4000, 10% 2-PROPANOL, 0.05 M NA HEPES BUFFER (PH=7.5), pH 7.50 Resolution 2.00 Å R-free 0.247

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 1CI8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CI9 DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI Deposited 1999-04-08 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–392（392 aa）
Chain B 1–392（392 aa）
Not recorded DFP DIISOPROPYL PHOSPHONATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；10% PEG 4000, 10% 2-PROPANOL, 0.05M NA HEPES BUFFER (PH=7.5), pH 7.50
Resolution 1.80 Å R-free 0.235

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

View Construct and Data Evidence
UniProt name Q9KX40_9BURK
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–392； UniProt 1–392 Author chain B； PDBConstruct 1–392； UniProt 1–392

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 1ci8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ci8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ci8
Deposition date deposition_date1999-04-08
Structure title titleESTERASE ESTB FROM BURKHOLDERIA GLADIOLI: AN ESTERASE WITH (BETA)-LACTAMASE FOLD.
Keywords keywordsESTERASE, LACTAMASE FOLD, 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_guinier29.99 Å
Radius of gyration Rg (electron density) rg_electron29.30 Å
Forward intensity I(0) i0104083000.00
Molecular weight molecular_weight80446.0 kDa
Excluded volume excluded_volume100640 ų
Envelope volume envelope_volume119320 ų
Hydration-shell volume shell_volume34295 ų
Envelope diameter envelope_diameter106.6 Å
Shell Rg shell_rg35.94 Å
Envelope Rg envelope_rg29.21 Å
Shape Rg shape_rg29.33 Å
Total Rg total_rg29.81 Å
Total atoms total_atoms5686
Residues n_residues754
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 dmax100.5 Å
Rg (real space) rg_real30.06 Å
Rg uncertainty (real space) rg_real_error0.70 Å
I(0) (real space) i0_real1.0410e+08
I(0) uncertainty (real space) i0_real_error1.5900e+06
Rg (reciprocal space) rg_reciprocal30.03 Å
I(0) (reciprocal space) i0_reciprocal104100000.0000
Solution quality estimate total_estimate0.8674
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3 Å
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.440
Angular range angular_range— – 0.2650 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41080000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.927
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ci8a_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase
Domain ID domain_idd1ci8b_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

CATH v4.4 (2 domains)

Domain ID domain_id1ci8A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
Domain ID domain_id1ci8B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
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8. Citations (2)

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9. Files and Curves (10)