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1a5c

FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM

Method: X-RAY DIFFRACTION Dmax: 95.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE

Plasmodium falciparum

UniProt P14223

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 2–369 Chain B； UniProt 2–369 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 7.6；VAPOR DIFFUSION: 2.0 M AMMONIUM SULFATE/5% 2-PROPANOL, pH 7.6, vapor diffusion Resolution 3.00 Å R-free 0.329

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 1A5C Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2EPH Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP-tail determined at 2.7 angstrom resolution Deposited 2007-03-30 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 1–369（369 aa）
Chain B 1–369（369 aa）
Chain C 1–369（369 aa）
Chain D 1–369（369 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；2.5 mM TRAP-tail, 0.5% n-dodecyl-beta-D-maltoside, 50 mM cacodylic acid pH 6.0, 20% PEG 2000, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.70 Å R-free 0.250
2PC4 Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP-tail determined at 2.4 angstrom resolution Deposited 2007-03-29 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 1–369（369 aa）
Chain B 1–369（369 aa）
Chain C 1–369（369 aa）
Chain D 1–369（369 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；2.5 mM TRAP-tail, 0.5% n-dodecyl-beta-D-maltoside, 50 mM Cacodylic acid pH 6.0, 20% PEG 2000, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.40 Å R-free 0.250

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ALF_PLAFA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–368； UniProt 2–369 Author chain B； PDBConstruct 1–368； UniProt 2–369

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 1a5c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a5c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a5c
Deposition date deposition_date1998-02-13
Structure title titleFRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM
Keywords keywordsFRUCTOSE-1, 6-BISPHOSPHATE ALDOLASE, MALARIA, TIM BARREL, LYASE; LYASE
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_guinier29.44 Å
Radius of gyration Rg (electron density) rg_electron28.77 Å
Forward intensity I(0) i085276500.00
Molecular weight molecular_weight73935.0 kDa
Excluded volume excluded_volume93199 ų
Envelope volume envelope_volume109110 ų
Hydration-shell volume shell_volume32230 ų
Envelope diameter envelope_diameter100.1 Å
Shell Rg shell_rg35.45 Å
Envelope Rg envelope_rg28.69 Å
Shape Rg shape_rg28.77 Å
Total Rg total_rg29.39 Å
Total atoms total_atoms5204
Residues n_residues684
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 dmax95.4 Å
Rg (real space) rg_real29.50 Å
Rg uncertainty (real space) rg_real_error0.70 Å
I(0) (real space) i0_real8.5280e+07
I(0) uncertainty (real space) i0_real_error1.3030e+06
Rg (reciprocal space) rg_reciprocal29.48 Å
I(0) (reciprocal space) i0_reciprocal85270000.0000
Solution quality estimate total_estimate0.8891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary— Å
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.549
Angular range angular_range— – 0.2700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16510000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.967
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a5ca_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.10 — Aldolase
Family Family familyc.1.10.1 — Class I aldolase
Domain ID domain_idd1a5cb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.10 — Aldolase
Family Family familyc.1.10.1 — Class I aldolase

CATH v4.4 (2 domains)

Domain ID domain_id1a5cA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily70 — Aldolase class I
Domain ID domain_id1a5cB00
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 (1)

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9. Files and Curves (10)