1xzf

FUSARIUM SOLANI CUTINASE MUTANT WITH THR 144 REPLACED BY CYS

Method: X-RAY DIFFRACTION Dmax: 53.8 Å Quality: GOOD

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

CUTINASE

Nectria haematococca mpVI

UniProt P00590

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 17–230 Mutation:T144C No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.69 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.

43 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUTI1_FUSSO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–214; UniProt 17–230

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 1xzf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xzf
Deposition date deposition_date1995-11-28
Structure title titleFUSARIUM SOLANI CUTINASE MUTANT WITH THR 144 REPLACED BY CYS
Keywords keywordsHYDROLASE, SERINE ESTERASE, GLYCOPROTEIN, HYDROLASE (SERINE ESTERASE); HYDROLASE (SERINE ESTERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.54
Radius of gyration Rg (electron density) rg_electron15.22
Forward intensity I(0) i08341550.00
Molecular weight molecular_weight20467.0 kDa
Excluded volume excluded_volume25363 ų
Envelope volume envelope_volume28046 ų
Hydration-shell volume shell_volume15253 ų
Envelope diameter envelope_diameter52.2
Shell Rg shell_rg21.51
Envelope Rg envelope_rg15.51
Shape Rg shape_rg15.19
Total Rg total_rg16.37
Total atoms total_atoms1773
Residues n_residues197
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 dmax53.8
Rg (real space) rg_real16.39
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real8.3420e+06
I(0) uncertainty (real space) i0_real_error9.2540e+04
Rg (reciprocal space) rg_reciprocal16.41
I(0) (reciprocal space) i0_reciprocal8342000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.379
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3240000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1xzfa_
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.69.1.30 — Cutinase-like

CATH v4.4 (1 domains)

Domain ID domain_id1xzfA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain

8. Citations (5)

9. Files and Curves (10)