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1btm

TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Method: X-RAY DIFFRACTION Dmax: 77.7 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 2–253 Chain B； UniProt 2–253 Not recorded PGA 2-PHOSPHOGLYCOLIC ACID × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å

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 1BTM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2BTM DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES? Deposited 1999-01-04 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–252（251 aa）
Chain B 2–252（251 aa）
Mutation：H12N, K13G, P230A 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

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 1–252； UniProt 2–253 Author chain B； PDBConstruct 1–252； UniProt 2–253

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 1btm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1btm
Deposition date deposition_date1995-11-11
Structure title titleTRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID
Keywords keywordsISOMERASE; 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_guinier25.05 Å
Radius of gyration Rg (electron density) rg_electron23.93 Å
Forward intensity I(0) i048474500.00
Molecular weight molecular_weight53797.0 kDa
Excluded volume excluded_volume67274 ų
Envelope volume envelope_volume74805 ų
Hydration-shell volume shell_volume26461 ų
Envelope diameter envelope_diameter78.6 Å
Shell Rg shell_rg31.14 Å
Envelope Rg envelope_rg24.01 Å
Shape Rg shape_rg23.96 Å
Total Rg total_rg24.64 Å
Total atoms total_atoms3781
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 dmax77.7 Å
Rg (real space) rg_real25.07 Å
Rg uncertainty (real space) rg_real_error0.45 Å
I(0) (real space) i0_real4.8470e+07
I(0) uncertainty (real space) i0_real_error6.3720e+05
Rg (reciprocal space) rg_reciprocal25.07 Å
I(0) (reciprocal space) i0_reciprocal48470000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1 Å
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.3150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12950000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.962
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1btma_
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_idd1btmb_
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_id1btmA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily70 — Aldolase class I
Domain ID domain_id1btmB00
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 (2)

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9. Files and Curves (10)