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2btm

DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?

Method: X-RAY DIFFRACTION Dmax: 77.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (TRIOSEPHOSPHATE ISOMERASE)

Geobacillus stearothermophilus

UniProt P00943

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 2–252 Chain B； UniProt 2–252 Mutation：H12N, K13G, P230A PGA 2-PHOSPHOGLYCOLIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5 Resolution 2.40 Å R-free 0.220

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.

Other PDB Difference from Current Entry 2BTM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BTM TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID Deposited 1995-11-11 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–253（252 aa）
Chain B 2–253（252 aa）
Not recorded PGA 2-PHOSPHOGLYCOLIC ACID × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPIS_BACST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–251； UniProt 2–252 Author chain B； PDBConstruct 1–251； UniProt 2–252

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 2btm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2btm
Deposition date deposition_date1999-01-04
Structure title titleDOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?
Keywords keywordsTHERMOPHILIC TRIOSE-PHOSPHATE, GLYCOLYSIS, ISOMERASE; ISOMERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.70 Å
Radius of gyration Rg (electron density) rg_electron23.65 Å
Forward intensity I(0) i045510400.00
Molecular weight molecular_weight52495.0 kDa
Excluded volume excluded_volume65861 ų
Envelope volume envelope_volume73180 ų
Hydration-shell volume shell_volume26140 ų
Envelope diameter envelope_diameter78.5 Å
Shell Rg shell_rg30.83 Å
Envelope Rg envelope_rg23.75 Å
Shape Rg shape_rg23.69 Å
Total Rg total_rg24.37 Å
Total atoms total_atoms3690
Residues n_residues502
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax77.1 Å
Rg (real space) rg_real24.72 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real4.5510e+07
I(0) uncertainty (real space) i0_real_error5.4030e+05
Rg (reciprocal space) rg_reciprocal24.72 Å
I(0) (reciprocal space) i0_reciprocal45510000.0000
Solution quality estimate total_estimate0.8991
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.9 Å
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.3200 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13230000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.955
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2btma_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.1 — Triosephosphate isomerase (TIM)
Family Family familyc.1.1.1 — Triosephosphate isomerase (TIM)
Domain ID domain_idd2btmb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.1 — Triosephosphate isomerase (TIM)
Family Family familyc.1.1.1 — Triosephosphate isomerase (TIM)

CATH v4.4 (2 domains)

Domain ID domain_id2btmA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily70 — Aldolase class I
Domain ID domain_id2btmB00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily70 — Aldolase class I
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8. Citations (3)

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9. Files and Curves (10)