4zb0

A dehydrated form of glucose isomerase collected at room temperature.

Method: X-RAY DIFFRACTION Dmax: 90.3 Å Quality: EXCELLENT

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 2–388 Chain B; UniProt 2–388 Fragment:UNP residues 2-388 MN MANGANESE (II) ION × 20 GLC alpha-D-glucopyranose × 4 FRU beta-D-fructofuranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.1 M Hepes, 10% PEG 400, 0.05 M Manganese Chloride, 20% Glucose Resolution 2.00 Å R-free 0.180

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 1–387; UniProt 2–388 Author chain B; PDBConstruct 1–387; UniProt 2–388

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 4zb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4zb0
Deposition date deposition_date2015-04-14
Structure title titleA dehydrated form of glucose isomerase collected at room temperature.
Keywords keywordsISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.12
Radius of gyration Rg (electron density) rg_electron27.90
Forward intensity I(0) i0131384000.00
Molecular weight molecular_weight87390.0 kDa
Excluded volume excluded_volume107790 ų
Envelope volume envelope_volume128930 ų
Hydration-shell volume shell_volume37622 ų
Envelope diameter envelope_diameter94.4
Shell Rg shell_rg36.14
Envelope Rg envelope_rg28.08
Shape Rg shape_rg27.88
Total Rg total_rg28.68
Total atoms total_atoms6172
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 dmax90.3
Rg (real space) rg_real29.04
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.3140e+08
I(0) uncertainty (real space) i0_real_error1.8310e+06
Rg (reciprocal space) rg_reciprocal29.07
I(0) (reciprocal space) i0_reciprocal131400000.0000
Solution quality estimate total_estimate0.9051
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33590000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4zb0a_
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
Domain ID domain_idd4zb0b_
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 (2 domains)

Domain ID domain_id4zb0A00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily150 — Divalent-metal-dependent TIM barrel enzymes
Domain ID domain_id4zb0B00
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)