Structure of PDB 5lu4 Chain B

Receptor sequence
>5lu4B (length=847) Species: 4227 (Flaveria trinervia) [Search protein sequence]
KKRVFTFGKGRSEGNRDMKSLLGGKGANLAEMSSIGLSVPPGLTISTEAC
EEYQQNGKSLPPGLWDEISEGLDYVQKEMSASLGDPSKPLLLSVRSGAAI
SMPGMMDTVLNLGLNDEVVAGLAGKSGARFAYDSYRRFLDMFGNVVMGIP
HSLFDEKLEQMKAEKGIHLDTDLTAADLKDLVEKYKNVYVEAKGEKFPTD
PKKQLELAVNAVFDSWDSPRANKYRSINQITGLKGTAVNIQSMVFGNMGN
TSGTGVLFTRNPSTGEKKLYGEFLINAQGEDVVAGIRTPEDLGTMETCMP
EAYKELVENCEILERHYKDMMDIEFTVQENRLWMLQCRTGKRTGKGAVRI
AVDMVNEGLIDTRTAIKRVETQHLDQLLHPQFEDPSAYKSHVVATGLPAS
PGAAVGQVCFSAEDAETWHAQGKSAILVRTETSPEDVGGMHAAAGILTAR
GGMTSHAAVVARGWGKCCVSGCADIRVNDDMKIFTIGDRVIKEGDWLSLN
GTTGEVILGKQLLAPPAMSNDLEIFMSWADQARRLKVMANADTPNDALTA
RNNGAQGIGLCRTEHMFFASDERIKAVRKMIMAVTPEQRKVALDLLLPYQ
RSDFEGIFRAMDGLPVTIRLLDPPLHEFLKIENLSEVNPMLGFRGCRLGI
SYPELTEMQVRAIFQAAVSMTNQGVTVIPEIMVPLVGTPQELRHQISVIR
GVAANVFAEMGVTLEYKVGTMIEIPRAALIAEEIGKEADFFSFGTNDLTQ
MTFGYSRDDVGKFLQIYLAQGILQHDPFEVIDQKGVGQLIKMATEKGRAA
NPSLKVGICGEHGGEPSSVAFFDGVGLDYVSCSPFRVPIARLAAAQV
3D structure
PDB5lu4 Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E723 S742 D747 C809 Y829
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 B 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 B E324 Q336 E324 Q336
BS03 MG B D622 E748 D772 D622 E723 D747
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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