1sf7

BINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY

Method: POWDER DIFFRACTION Dmax: 52.8 Å Quality: GOOD

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

LYSOZYME

Gallus gallus

UniProt P00698

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 19–147 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-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 POWDER DIFFRACTION X-ray crystallization conditions:rapid precipitation;pH 6;298 K;NaCl, Na2HPO4, KH2PO4, tetra-N-acetylchitotetraose, pH 6.0, rapid precipitation, temperature 298K Resolution 3.22 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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 19–147

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 1sf7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sf7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sf7
Deposition date deposition_date2004-02-19
Structure title titleBINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY
Keywords keywordsPOWDER DIFFRACTION; RIETVELD REFINEMENT; LYSOZYME, HYDROLASE; HYDROLASE
Experimental Method methodPOWDER DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.88
Radius of gyration Rg (electron density) rg_electron14.56
Forward intensity I(0) i05293340.00
Molecular weight molecular_weight15155.0 kDa
Excluded volume excluded_volume18459 ų
Envelope volume envelope_volume22159 ų
Hydration-shell volume shell_volume13065 ų
Envelope diameter envelope_diameter52.6
Shell Rg shell_rg20.12
Envelope Rg envelope_rg14.65
Shape Rg shape_rg14.54
Total Rg total_rg15.70
Total atoms total_atoms1058
Residues n_residues129
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 dmax52.8
Rg (real space) rg_real15.78
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real5.2930e+06
I(0) uncertainty (real space) i0_real_error5.6660e+04
Rg (reciprocal space) rg_reciprocal15.80
I(0) (reciprocal space) i0_reciprocal5293000.0000
Solution quality estimate total_estimate0.8758
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.1
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha840800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1sf7a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme

8. Citations (4)

9. Files and Curves (10)