Structure of PDB 6hl7 Chain C

Receptor sequence
>6hl7C (length=322) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
MFYINSKYKIDLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILK
NNEDSKYLENKVFCSVFLEPSTATRCSFDAAILKLGSKVLNITDGETVED
AFKILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLD
FYTIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNF
VSCKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMT
RINAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQAENG
LYVRMALLYLIFSSTWSHPQFE
3D structure
PDB6hl7 Molecular Target Validation of Aspartate Transcarbamoylase fromPlasmodium falciparumby Torin 2.
ChainC
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R159 H187 Q190 T294 P333 G359
Catalytic site (residue number reindexed from 1) R115 H143 Q146 T250 P274 G300
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 CP C S107 T110 R159 H187 R226 L334 S71 T74 R115 H143 R182 L275
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6hl7, PDBe:6hl7, PDBj:6hl7
PDBsum6hl7
PubMed32129597
UniProtO15804

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