Structure of PDB 5wml Chain A Binding Site BS01

Receptor Information
>5wml Chain A (length=404) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEPDFDTPKVVAE
AGINAIREGFTRYTLNAGITELREAICRKLKEENGLSYAPDQILVSNGAK
QSLLQAVLAVCSPGDEVIIPAPYWVSYTEQARLADATPVVIPTKISNNFL
LDPKDLESKLTEKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLV
LSDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSAAFAMTGWRLGYLA
GPKHIVAACSKLQGQVSSGASSIAQKAGVAALGLGKAGGETVAEMVKAYR
ERRDFLVKSLGDIKGVKISEPQGAFYLFIDFSAYYGSEAEGFGLINDSSS
LALYFLDKFQVAMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL
RATV
Ligand information
Ligand IDPMP
InChIInChI=1S/C8H13N2O5P/c1-5-8(11)7(2-9)6(3-10-5)4-15-16(12,13)14/h3,11H,2,4,9H2,1H3,(H2,12,13,14)
InChIKeyZMJGSOSNSPKHNH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1CN)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN)c1O
FormulaC8 H13 N2 O5 P
Name4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE;
PYRIDOXAMINE-5'-PHOSPHATE
ChEMBLCHEMBL1235353
DrugBankDB02142
ZINCZINC000001532708
PDB chain5wml Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5wml Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.
Resolution2.103 Å
Binding residue
(original residue number in PDB)		G167 A168 K169 L172 W193 N243 D272 Y275 S305 R314
Binding residue
(residue number reindexed from 1)		G98 A99 K100 L103 W124 N174 D203 Y206 S236 R245
Annotation score1
Enzymatic activity
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.78: aspartate--prephenate aminotransferase.
2.6.1.79: glutamate--prephenate aminotransferase.
Gene Ontology
Molecular Function
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0033853 aspartate-prephenate aminotransferase activity
GO:0033854 glutamate-prephenate aminotransferase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0009095 aromatic amino acid family biosynthetic process, prephenate pathway
GO:0009793 embryo development ending in seed dormancy
Cellular Component
GO:0005829 cytosol
GO:0009507 chloroplast
GO:0009570 chloroplast stroma

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5wml, PDBe:5wml, PDBj:5wml
PDBsum5wml
PubMed29405514
UniProtQ9SIE1|PAT_ARATH Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase (Gene Name=PAT)

[Back to BioLiP]