Structure of PDB 5uyy Chain A

Receptor sequence
>5uyyA (length=373) Species: 1392 (Bacillus anthracis) [Search protein sequence]
ESLEMRQMRKKVVLIGTGLIGGSLALAIKKDHDVTITGYDIFQEQVERAK
ELHVVDEIAVDLQHACEEAHLIVFASPVEETKKLLHKLASFHLREDVIVT
DVGSTKGSIMNEAEALFSKEISFIGGHPMAGSHKTGVESAKAHLFENAFY
ILTPMHHVPNEHVEELKDWLKGTGSHFLVLNTEEHDYVTGIVSHFPHLIA
AGLVKQVEKHAGDNPLIHQLAAGGFKDITRIASSSPKMWSDIVKQNREHL
MVLLKEWISEMEDLYDTVSSGDAGEIQNYFADAKEYRDSLPVRKRGAIPA
YHDLYVDVLDKVGALAHVTSILAREEISITNLQILEAREGLLGVLRISFQ
REEDRMKAKLALGEEKYQTYETI
3D structure
PDB5uyy Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.
ChainA
Resolution2.6 Å
3D
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
Enzyme Commision number 1.3.1.12: prephenate dehydrogenase.
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 TYR A L314 D315 K316 A319 L320 E341 G348 L309 D310 K311 A314 L315 E336 G343
BS02 TYR A N152 I334 N147 I329
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004665 prephenate dehydrogenase (NADP+) activity
GO:0008977 prephenate dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0070403 NAD+ binding
Biological Process
GO:0006571 tyrosine biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5uyy, PDBe:5uyy, PDBj:5uyy
PDBsum5uyy
PubMed31750992
UniProtQ81P63

[Back to BioLiP]