Structure of PDB 5lu4 Chain A

Receptor sequence
>5lu4A (length=850) Species: 4227 (Flaveria trinervia) [Search protein sequence]
KKRVFTFGKGRSEGNRDMKSLLGGKGANLAEMSSIGLSVPPGLTISTEAC
EEYQQNGKSLPPGLWDEISEGLDYVQKEMSASLGDPSKPLLLSVRSGAAI
SMPGMMDTVLNLGLNDEVVAGLAGKSGARFAYDSYRRFLDMFGNVVMGIP
HSLFDEKLEQMKAEKGIHLDTDLTAADLKDLVEKYKNVYVEAKGEKFPTD
PKKQLELAVNAVFDSWDSPRANKYRSINQITGLKGTAVNIQSMVFGNMGN
TSGTGVLFTRNPSTGEKKLYGEFLINAQGEDVVAGIRTPEDLGTMETCMP
EAYKELVENCEILERHYKDMMDIEFTVQENRLWMLQCRTGKRTGKGAVRI
AVDMVNEGLIDTRTAIKRVETQHLDQLLHPQFEDPSAYKSHVVATGLPAS
PGAAVGQVCFSAEDAETWHAQGKSAILVRTETSPEDVGGMHAAAGILTAR
GGMTSHAAVVARGWGKCCVSGCADIRVNDDMKIFTIGDRVIKEGDWLSLN
GTTGEVILGKQLLAPPAMSNDLEIFMSWADQARRLKVMANADTPNDALTA
RNNGAQGIGLCRTEHMFFASDERIKAVRKMIMAVTPEQRKVALDLLLPYQ
RSDFEGIFRAMDGLPVTIRLLDPPLHEFLIYSKIENLSEVNPMLGFRGCR
LGISYPELTEMQVRAIFQAAVSMTNQGVTVIPEIMVPLVGTPQELRHQIS
VIRGVAANVFAEMGVTLEYKVGTMIEIPRAALIAEEIGKEADFFSFGTND
LTQMTFGYSRDDVGKFLQIYLAQGILQHDPFEVIDQKGVGQLIKMATEKG
RAANPSLKVGICGEHGGEPSSVAFFDGVGLDYVSCSPFRVPIARLAAAQV
3D structure
PDB5lu4 Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the 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
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.
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 ADP A K25 S93 R95 T108 L110 S242 M243 V244 G279 E280 E324 L335 Q336 K25 S93 R95 T108 L110 S242 M243 V244 G279 E280 E324 L335 Q336
BS02 MG A E324 Q336 E324 Q336
BS03 PYR A E748 G769 N771 D772 E726 G747 N749 D750
BS04 MG A D622 E748 D772 D622 E726 D750
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

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

[Back to BioLiP]