Structure of PDB 5lu4 Chain A Binding Site BS03

Receptor Information
>5lu4 Chain A (length=850) Species: 4227 (Flaveria trinervia) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KKRVFTFGKGRSEGNRDMKSLLGGKGANLAEMSSIGLSVPPGLTISTEAC
EEYQQNGKSLPPGLWDEISEGLDYVQKEMSASLGDPSKPLLLSVRSGAAI
SMPGMMDTVLNLGLNDEVVAGLAGKSGARFAYDSYRRFLDMFGNVVMGIP
HSLFDEKLEQMKAEKGIHLDTDLTAADLKDLVEKYKNVYVEAKGEKFPTD
PKKQLELAVNAVFDSWDSPRANKYRSINQITGLKGTAVNIQSMVFGNMGN
TSGTGVLFTRNPSTGEKKLYGEFLINAQGEDVVAGIRTPEDLGTMETCMP
EAYKELVENCEILERHYKDMMDIEFTVQENRLWMLQCRTGKRTGKGAVRI
AVDMVNEGLIDTRTAIKRVETQHLDQLLHPQFEDPSAYKSHVVATGLPAS
PGAAVGQVCFSAEDAETWHAQGKSAILVRTETSPEDVGGMHAAAGILTAR
GGMTSHAAVVARGWGKCCVSGCADIRVNDDMKIFTIGDRVIKEGDWLSLN
GTTGEVILGKQLLAPPAMSNDLEIFMSWADQARRLKVMANADTPNDALTA
RNNGAQGIGLCRTEHMFFASDERIKAVRKMIMAVTPEQRKVALDLLLPYQ
RSDFEGIFRAMDGLPVTIRLLDPPLHEFLIYSKIENLSEVNPMLGFRGCR
LGISYPELTEMQVRAIFQAAVSMTNQGVTVIPEIMVPLVGTPQELRHQIS
VIRGVAANVFAEMGVTLEYKVGTMIEIPRAALIAEEIGKEADFFSFGTND
LTQMTFGYSRDDVGKFLQIYLAQGILQHDPFEVIDQKGVGQLIKMATEKG
RAANPSLKVGICGEHGGEPSSVAFFDGVGLDYVSCSPFRVPIARLAAAQV
Ligand information
Ligand IDPYR
InChIInChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
InChIKeyLCTONWCANYUPML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)C(O)=O
OpenEye OEToolkits 1.7.6CC(=O)C(=O)O
ACDLabs 12.01O=C(C(=O)O)C
FormulaC3 H4 O3
NamePYRUVIC ACID
ChEMBLCHEMBL1162144
DrugBankDB00119
ZINCZINC000001532517
PDB chain5lu4 Chain A Residue 903 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5lu4 Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		E748 G769 N771 D772
Binding residue
(residue number reindexed from 1)		E726 G747 N749 D750
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K25 R95 G104 M106 R338 H456 E748 S767 D772 C834 Y854
Catalytic site (residue number reindexed from 1) K25 R95 G104 M106 R338 H456 E726 S745 D750 C812 Y832
Enzyme Commision number 2.7.9.1: pyruvate, phosphate dikinase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0046872 metal ion binding
GO:0050242 pyruvate, phosphate dikinase activity
Biological Process
GO:0006090 pyruvate metabolic process
GO:0015979 photosynthesis
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0009507 chloroplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5lu4, PDBe:5lu4, PDBj:5lu4
PDBsum5lu4
PubMed28470715
UniProtP22221|PPDK_FLATR Pyruvate, phosphate dikinase, chloroplastic (Gene Name=PPDK)

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