Structure of PDB 6ypo Chain B

Receptor sequence
>6ypoB (length=311) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
HMFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATL
FYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVEG
YSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSE
IGKLDGISVALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDI
KDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERLDLYEAARGK
FIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIR
MALLKLLLVGW
3D structure
PDB6ypo Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase.
ChainB
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R187 H215 Q218 T309 P349 G375
Catalytic site (residue number reindexed from 1) R108 H136 Q139 T230 P270 G296
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 U5P B R136 T137 R187 H215 R248 T249 R310 H348 P349 L350 P351 R57 T58 R108 H136 R169 T170 R231 H269 P270 L271 P272
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6ypo, PDBe:6ypo, PDBj:6ypo
PDBsum6ypo
PubMed33574254
UniProtP49077|PYRB_ARATH Aspartate carbamoyltransferase, chloroplastic (Gene Name=PYRB)

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