Structure of PDB 6f5v Chain D Binding Site BS01

Receptor Information
>6f5v Chain D (length=403) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVDMSLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEPDFDTPKV
VAEAGINAIREGFTRYTLNAGITELREAICRKLKEENGLSYAPDQILVSN
GAKQSLLQAVLAVCSPGDEVIIPAPYWVSYTEQARLADATPVVIPTKISN
NFLLDPKDLESKLTEKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPR
LLVLSDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAMTGWRLG
YLAGPKHIVAACSKLQGQVSSGASSIAQKAGVAALGLGKAGGETVAEMVK
AYRERRDFLVKSLGDIKGVKISEPQGAFYLFIDFSAYYGSEAEGFGLIND
SSSLALYFLDKFQVAMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKAL
EPL
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 chain6f5v Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6f5v Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1 beta aspartate aminotransferase.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		G120 A121 K122 W146 N196 D225 I227 Y228 S258 K259 R267
Binding residue
(residue number reindexed from 1)		G101 A102 K103 W127 N177 D206 I208 Y209 S239 K240 R248
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:6f5v, PDBe:6f5v, PDBj:6f5v
PDBsum6f5v
PubMed30771275
UniProtQ9SIE1|PAT_ARATH Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase (Gene Name=PAT)

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