2gve

Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase

Method: NEUTRON DIFFRACTION Dmax: 108.9 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 1–387 Not recorded CO COBALT (II) ION × 8 NEUTRON DIFFRACTION X-ray crystallization conditions:LIQUID DIFFUSION;pH 8;293 K;50mM tris-HCl,38%AMSO4,2mM Mn2+ and 2mM Co2+,XI @ 125mg/ml, pH 8.0, LIQUID DIFFUSION, temperature 293K Resolution 2.20 Å R-free 0.319

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 2–388; 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 2gve

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gve
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gve
Deposition date deposition_date2006-05-02
Structure title titleTime-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase
Keywords keywordsTIM barrel-beta-alpha-barrels, two metal binding sites, protonation states of residues, ISOMERASE; ISOMERASE
Experimental Method methodNEUTRON DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.90
Radius of gyration Rg (electron density) rg_electron24.95
Forward intensity I(0) i057727400.00
Molecular weight molecular_weight53657.0 kDa
Excluded volume excluded_volume64157 ų
Envelope volume envelope_volume109750 ų
Hydration-shell volume shell_volume33434 ų
Envelope diameter envelope_diameter116.8
Shell Rg shell_rg34.28
Envelope Rg envelope_rg28.93
Shape Rg shape_rg25.78
Total Rg total_rg23.65
Total atoms total_atoms7364
Residues n_residues388
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 dmax108.9
Rg (real space) rg_real27.04
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real5.7730e+07
I(0) uncertainty (real space) i0_real_error8.8850e+05
Rg (reciprocal space) rg_reciprocal26.99
I(0) (reciprocal space) i0_reciprocal57730000.0000
Solution quality estimate total_estimate0.7511
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.564
Kurtosis Kurtosis kurtosis0.166
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14570000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.423; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.494; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2gvea_
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_id2gveA00
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 (2)

9. Files and Curves (10)