Structure of PDB 6fba Chain C

Receptor sequence

>6fbaC (length=328) Species: 5833 (Plasmodium falciparum)

DLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLEN
KVFCSVFLEPSTRTRCSFDAAILKLGSKVLNITDMNSTSFYKGETVEDAF
KILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFY
TIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVS
CKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMTRI
QKERFTDVDEYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDS
NPKSVYFTQAENGLYVRMALLYLIFSST

3D structure

• PDB: 6fba Identification of a non-competitive inhibitor of Plasmodium falciparum aspartate transcarbamoylase.
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R109 T110 K138 R159 H187 Q190 T294 P333 G359
• Catalytic site (residue number reindexed from 1): R63 T64 K92 R113 H141 Q144 T248 P287 G313
• Enzyme Commision number: 2.1.3.2: aspartate carbamoyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	D48	C	E140 I148 L149	E94 I102 L103	MOAD: Kd=19.9uM

Gene Ontology

Molecular Function

• GO:0004070 aspartate carbamoyltransferase activity
• GO:0016597 amino acid binding
• GO:0016740 transferase activity
• GO:0016743 carboxyl- or carbamoyltransferase activity

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0006520 amino acid metabolic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:6fba, PDBe:6fba, PDBj:6fba
• PDBsum: 6fba
• PubMed: 29476738
• UniProt: O15804