4e3v

Crystal Structure of XYLOSE ISOMERASE FROM STREPTOMYCES RUBIGINOSUS Cryoprotected in Proline

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: REASONABLE

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

Xylose isomerase

OrganismNot specified

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 Not recorded PRO PROLINE × 4 SO4 SULFATE ION × 8 MG MAGNESIUM ION × 4 MN MANGANESE (II) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;294 K;2.0M ammonium sulfate, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K Resolution 1.50 Å R-free 0.179

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

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 4e3v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4e3v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4e3v
Deposition date deposition_date2012-03-10
Structure title titleCrystal Structure of XYLOSE ISOMERASE FROM STREPTOMYCES RUBIGINOSUS Cryoprotected in Proline
Keywords keywordsISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.44
Radius of gyration Rg (electron density) rg_electron23.33
Forward intensity I(0) i033268700.00
Molecular weight molecular_weight42811.0 kDa
Excluded volume excluded_volume52910 ų
Envelope volume envelope_volume67694 ų
Hydration-shell volume shell_volume24787 ų
Envelope diameter envelope_diameter87.5
Shell Rg shell_rg29.51
Envelope Rg envelope_rg24.20
Shape Rg shape_rg23.31
Total Rg total_rg24.10
Total atoms total_atoms3021
Residues n_residues385
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 dmax84.2
Rg (real space) rg_real24.54
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real3.3270e+07
I(0) uncertainty (real space) i0_real_error4.6480e+05
Rg (reciprocal space) rg_reciprocal24.51
I(0) (reciprocal space) i0_reciprocal33270000.0000
Solution quality estimate total_estimate0.6880
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis-0.095
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5465000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 0.264; Positv: 1.000; Valcen: 0.911; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4e3va_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.15 — Xylose isomerase-like
Family Family familyc.1.15.3 — Xylose isomerase

CATH v4.4 (1 domains)

Domain ID domain_id4e3vA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily150 — Divalent-metal-dependent TIM barrel enzymes

8. Citations (1)

9. Files and Curves (10)