1A5C	Lyase	date	Feb 13, 1998
title	Fructose-1,6-Bisphosphate Aldolase From Plasmodium Falciparum
authors	H.Kim, U.Certa, H.Dobeli, P.Jakob, W.G.J.Hol
compound		source
Molecule: Fructose-1,6-Bisphosphate Aldolase Chain: A, B Synonym: Pfaldo Ec: 4.1.2.13 Engineered: Yes		Organism_scientific: Plasmodium Falciparum Expression_system: Escherichia Coli
symmetry	Space Group: P 32 2 1	R_factor	0.239
crystal cell	length a length b length c angle alpha angle beta angle gamma 119.200 119.200 132.300 90.00 90.00 120.00
method	X-Ray Diffraction	resolution	3.00 Å
ligand		enzyme	Fructose-bisphosphate aldolase;. Aldolase;. Fructose-1,6-bisphosphate triosephosphate-lyase;. Fructose diphosphate aldolase;. Diphosphofructose aldolase;. Fructose 1,6-diphosphate aldolase;. Ketose 1-phosphate aldolase;. Phosphofructoaldolase;. Zymohexase;. Fructoaldolase;. Fructose 1-phosphate aldolase;. Fructose 1-monophosphate aldolase;. 1,6-Diphosphofructose aldolase;. SMALDO. Lyase E.C.4.1.2.13 BRENDA
note	1A5C is a representative structure
similarity	Belongs to the class i fructose-bisphosphate aldolase family.[Glycolytic]
subunit	Homotetramer.
catalytic activ.	D-fructose 1,6-bisphosphate = glycerone phosphate + d-glyceraldehyde 3-phosphate.
pathway	Carbohydrate degradation; glycolysis; d-glyceraldehyde 3- phosphate and glycerone phosphate from d-glucose: step 4.
Gene Ontology	Chain Function Process Component A, B catalytic activity fructose-bisphosphate aldola... lyase activity glycolysis metabolic process
Primary reference	Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum., Kim H, Certa U, Dobeli H, Jakob P, Hol WG, Biochemistry 1998 Mar 31;37(13):4388-96. PMID:9521758

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (108 Kb) [Save to disk] Biological Unit Coordinates (1a5c.pdb1.gz) 208 Kb CSU: Contacts of Structural Units for 1A5C Likely Quarternary Molecular Structure file(s) for 1A5C Retrieve 1A5C in mmCIF format [Save to disk]

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1A5C, from MSDmotif at EBI Genome occurence of 1A5C's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1a5ca_, region A [Jmol] [rasmolscript] [script source]     - Domain d1a5cb_, region B [Jmol] [rasmolscript] [script source] Fold representative 1a5c from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1a5c_B] [1a5c_A]

Other resources with information on 1A5C

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