Structure of PDB 5wmh Chain F Binding Site BS01

Receptor Information
>5wmh Chain F (length=397) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DMSLSPRVQSLTMVITDLAATLVQSGVPVIRLAAGEPDFDTPKVVAEAGI
NAIREGFTRYTLNAGITELREAICRKLKEENGLSYAPDQILVSNGAKQSL
LQAVLAVCSPGDEVIIPAPYWVSYTEQARLADATPVVIPTKISNNFLLDP
KDLESKLTEKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLVLSD
EIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAMTGWRLGYLAGPK
HIVAACSKLQGQVSSGASSIAQKAGVAALGLGKAGGETVAEMVKAYRERR
DFLVKSLGDIKGVKISEPQGAFYLFIDFSAYYGSEAEGFGLINDSSSLAL
YFLDKFQVAMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain5wmh Chain F Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5wmh Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		G167 A168 K169 W193 D272 I274 S305 K306
Binding residue
(residue number reindexed from 1)		G95 A96 K97 W121 D200 I202 S233 K234
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:0003824 catalytic activity
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5wmh, PDBe:5wmh, PDBj:5wmh
PDBsum5wmh
PubMed29405514
UniProtQ9SIE1|PAT_ARATH Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase (Gene Name=PAT)

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