1oad

Glucose isomerase from Streptomyces rubiginosus in P21212 crystal form

Method: X-RAY DIFFRACTION Dmax: 97.8 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 2–388 Chain B; UniProt 2–388 Not recorded MN MANGANESE (II) ION × 4 MG MAGNESIUM ION × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MQD 2-METHYLPENTANE-1,2,4-TRIOL × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;17 MG/ML PROTEIN, 12 % MPD, 0.1 M MGCL2, 50 MM TRIS BUFFER PH 7.0 Resolution 1.50 Å R-free 0.186

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 2–388 Author chain B; PDBConstruct 2–388; 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 1oad

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1oad
Deposition date deposition_date2003-01-08
Structure title titleGlucose isomerase from Streptomyces rubiginosus in P21212 crystal form
Keywords keywordsISOMERASE, GLUCOSE ISOMERASE, XYLOSE ISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.07
Radius of gyration Rg (electron density) rg_electron29.96
Forward intensity I(0) i0127513000.00
Molecular weight molecular_weight86868.0 kDa
Excluded volume excluded_volume107620 ų
Envelope volume envelope_volume146180 ų
Hydration-shell volume shell_volume39646 ų
Envelope diameter envelope_diameter103.1
Shell Rg shell_rg37.70
Envelope Rg envelope_rg30.71
Shape Rg shape_rg29.95
Total Rg total_rg30.68
Total atoms total_atoms6133
Residues n_residues773
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 dmax97.8
Rg (real space) rg_real30.99
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.2750e+08
I(0) uncertainty (real space) i0_real_error1.8030e+06
Rg (reciprocal space) rg_reciprocal31.03
I(0) (reciprocal space) i0_reciprocal127500000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29400000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1oada_
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_idd1oadb_
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_id1oadA00
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_id1oadB00
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)