4zbc

A dehydrated form of glucose isomerase collected at 100K.

Method: X-RAY DIFFRACTION Dmax: 90.7 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 1–387 Chain B; UniProt 1–387 Not recorded MN MANGANESE (II) ION × 22 GLC alpha-D-glucopyranose × 8 FRU beta-D-fructofuranose × 8 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 0.182

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

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 4zbc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4zbc
Deposition date deposition_date2015-04-14
Structure title titleA dehydrated form of glucose isomerase collected at 100K.
Keywords keywordsISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.79
Radius of gyration Rg (electron density) rg_electron27.62
Forward intensity I(0) i0133748000.00
Molecular weight molecular_weight88166.0 kDa
Excluded volume excluded_volume108680 ų
Envelope volume envelope_volume126980 ų
Hydration-shell volume shell_volume37364 ų
Envelope diameter envelope_diameter94.8
Shell Rg shell_rg36.01
Envelope Rg envelope_rg27.83
Shape Rg shape_rg27.63
Total Rg total_rg28.34
Total atoms total_atoms6197
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 dmax90.7
Rg (real space) rg_real28.71
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.3370e+08
I(0) uncertainty (real space) i0_real_error1.9370e+06
Rg (reciprocal space) rg_reciprocal28.74
I(0) (reciprocal space) i0_reciprocal133800000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary89.0
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36860000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4zbca1
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_idd4zbca2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4zbcb1
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_idd4zbcb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4zbcA00
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_id4zbcB00
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)