Structure of PDB 6jks Chain F

Receptor sequence
>6jksF (length=318) Species: 353153 (Trypanosoma cruzi strain CL Brener) [Search protein sequence]
GSMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNL
LQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLAD
TIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLD
TLTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPD
ALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQDAAA
LQSFAAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFR
QMRYGMFMRMAILWSVLA
3D structure
PDB6jks Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism
ChainF
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R113 H141 Q144 T241 P287 G313
Catalytic site (residue number reindexed from 1) R115 H143 Q146 T243 P279 G305
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 F S62 S63 R64 T65 R113 H141 P287 L288 S64 S65 R66 T67 R115 H143 P279 L280
BS02 ASP F R113 R174 T175 L288 R115 R176 T177 L280
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6jks, PDBe:6jks, PDBj:6jks
PDBsum6jks
PubMed
UniProtQ4D3W3

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