Structure of PDB 6ysp Chain B

Receptor sequence
>6yspB (length=312) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
PHMFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMAT
LFYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVE
GYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQS
EIGKLDGISVALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDD
IKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERLDLYEAARG
KFIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFI
RMALLKLLLVGW
3D structure
PDB6ysp Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase.
ChainB
Resolution1.38 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) R187 H215 Q218 T309 P349 G375
Catalytic site (residue number reindexed from 1) R109 H137 Q140 T231 P271 G297
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 B S134 T135 R136 T137 R187 H215 Q218 P349 L350 S56 T57 R58 T59 R109 H137 Q140 P271 L272
BS02 PAL B S163 K166 S85 K88
Gene Ontology
Molecular Function
GO:0004070 aspartate carbamoyltransferase activity
GO:0016597 amino acid binding
GO:0016743 carboxyl- or carbamoyltransferase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006520 amino acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6ysp, PDBe:6ysp, PDBj:6ysp
PDBsum6ysp
PubMed33574254
UniProtP49077|PYRB_ARATH Aspartate carbamoyltransferase, chloroplastic (Gene Name=PYRB)

[Back to BioLiP]