Structure of PDB 6jkr Chain A

Receptor sequence
>6jkrA (length=322) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
SMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLL
QGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLADT
IRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDT
LTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDA
LQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKERFD
DAAALQSFAAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADPRA
AYFRQMRYGMFMRMAILWSVLA
3D structure
PDB6jkr Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism
ChainA
Resolution1.6 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 P283 G309
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 A S62 S63 R64 T65 R113 H141 Q144 P287 L288 S63 S64 R65 T66 R114 H142 Q145 P283 L284
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:6jkr, PDBe:6jkr, PDBj:6jkr
PDBsum6jkr
PubMed
UniProtO15636

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