Structure of PDB 6jl5 Chain F

Receptor sequence
>6jl5F (length=324) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
ELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNLLQGR
IMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLADTIRT
LDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLDTLTI
HSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPDALQM
PQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQKERFMAST
SDDAAALQSFAAKADITIDAARMRLAKEKMIVMHPLPRNDELSTTVDADP
RAAYFRQMRYGMFMRMAILWSVLA
3D structure
PDB6jl5 Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism
ChainF
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R113 H141 Q144 T241 P287 G313
Catalytic site (residue number reindexed from 1) R111 H139 Q142 T239 P285 G311
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 ASP F R113 H141 R174 T175 R242 Q244 L288 R111 H139 R172 T173 R240 Q242 L286
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6jl5, PDBe:6jl5, PDBj:6jl5
PDBsum6jl5
PubMed
UniProtO15636

[Back to BioLiP]