154l

THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE

Method: X-RAY DIFFRACTION Dmax: 49.6 Å Quality: GOOD

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

GOOSE LYSOZYME

OrganismNot specified

UniProt P00718

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 1–185 Not recorded ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.60 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.

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

View Construct and Data Evidence
UniProt name LYG_ANSAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–185; UniProt 1–185

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 154l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 154l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id154l
Deposition date deposition_date1994-05-05
Structure title titleTHE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE
Keywords keywordsHYDROLASE(O-GLYCOSYL); HYDROLASE(O-GLYCOSYL)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.16
Radius of gyration Rg (electron density) rg_electron15.07
Forward intensity I(0) i08677810.00
Molecular weight molecular_weight21014.0 kDa
Excluded volume excluded_volume26050 ų
Envelope volume envelope_volume27894 ų
Hydration-shell volume shell_volume15252 ų
Envelope diameter envelope_diameter49.7
Shell Rg shell_rg21.39
Envelope Rg envelope_rg15.31
Shape Rg shape_rg15.04
Total Rg total_rg16.18
Total atoms total_atoms1475
Residues n_residues185
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 dmax49.6
Rg (real space) rg_real16.01
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real8.6780e+06
I(0) uncertainty (real space) i0_real_error9.2280e+04
Rg (reciprocal space) rg_reciprocal16.02
I(0) (reciprocal space) i0_reciprocal8678000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.022
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2558000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd154la_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.5 — G-type lysozyme

CATH v4.4 (1 domains)

Domain ID domain_id154lA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)