Structure of PDB 6jkt Chain E

Receptor sequence
>6jktE (length=327) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
SMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLL
QGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLADT
IRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDT
LTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDA
LQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKERFM
ASTSDDAAALQSFAAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVD
ADPRAAYFRQMRYGMFMRMAILWSVLA
3D structure
PDB6jkt Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism
ChainE
Resolution2.3 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) R114 H142 Q145 T242 P288 G314
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 PAL E S89 K92 S90 K93
BS02 PAL E S62 S63 R64 T65 R113 H141 R174 T175 R242 Q244 L288 S63 S64 R65 T66 R114 H142 R175 T176 R243 Q245 L289
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
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Biological Process
External links
PDB RCSB:6jkt, PDBe:6jkt, PDBj:6jkt
PDBsum6jkt
PubMed
UniProtO15636

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