1mnz

Atomic structure of Glucose isomerase

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: GOOD

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 0–387 Not recorded MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.5;295 K;MPD, Magnesium chloride, Tris base, pH 7.5, EVAPORATION, temperature 295K Resolution 0.99 Å R-free 0.134

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 0–387

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 1mnz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mnz
Deposition date deposition_date2002-09-06
Structure title titleAtomic structure of Glucose isomerase
Keywords keywordshigh resolution, alpha/beta barrel, GI fold, ISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.73
Radius of gyration Rg (electron density) rg_electron23.59
Forward intensity I(0) i033816800.00
Molecular weight molecular_weight43365.0 kDa
Excluded volume excluded_volume53702 ų
Envelope volume envelope_volume69810 ų
Hydration-shell volume shell_volume25304 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg29.78
Envelope Rg envelope_rg24.40
Shape Rg shape_rg23.58
Total Rg total_rg24.35
Total atoms total_atoms3063
Residues n_residues387
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 dmax86.3
Rg (real space) rg_real24.83
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real3.3820e+07
I(0) uncertainty (real space) i0_real_error4.7610e+05
Rg (reciprocal space) rg_reciprocal24.81
I(0) (reciprocal space) i0_reciprocal33820000.0000
Solution quality estimate total_estimate0.8471
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.106
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6169000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.889; Smooth: 0.936

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_idd1mnza_
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_id1mnzA00
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)