8awf

Xylose Isomerase in 80% relative humidity environment

Method: X-RAY DIFFRACTION Dmax: 96.4 Å Quality: GOOD

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

Xylose isomerase

Streptomyces rubiginosus

UniProt P24300

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–388 Chain B; UniProt 1–388 Not recorded GOL GLYCEROL × 4 MN MANGANESE (II) ION × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 7.5;293 K;100 mM HEPES 200 mM Lithium Sulphate 34% Peg3350 Resolution 1.61 Å R-free 0.202

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.

139 other PDB entries and 143 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XYLA_STRRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–388; UniProt 1–388 Author chain B; PDBConstruct 1–388; UniProt 1–388

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 8awf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8awf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8awf
Deposition date deposition_date2022-08-29
Structure title titleXylose Isomerase in 80% relative humidity environment
Keywords keywordsXylose Isomerase, Glucose Isomerase, Humidity, Space group change, Unit cell change, ISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.08
Radius of gyration Rg (electron density) rg_electron30.04
Forward intensity I(0) i0127528000.00
Molecular weight molecular_weight86497.0 kDa
Excluded volume excluded_volume106940 ų
Envelope volume envelope_volume142520 ų
Hydration-shell volume shell_volume39182 ų
Envelope diameter envelope_diameter101.4
Shell Rg shell_rg37.54
Envelope Rg envelope_rg30.00
Shape Rg shape_rg30.04
Total Rg total_rg30.72
Total atoms total_atoms6108
Residues n_residues774
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 dmax96.4
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.2750e+08
I(0) uncertainty (real space) i0_real_error1.9090e+06
Rg (reciprocal space) rg_reciprocal31.04
I(0) (reciprocal space) i0_reciprocal127500000.0000
Solution quality estimate total_estimate0.8952
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.518
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47360000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)