Structure of PDB 1kc7 Chain A

Receptor sequence
>1kc7A (length=872) Species: 1512 ([Clostridium] symbiosum) [Search protein sequence]
AKWVYKFEEGNASMRNLLGGKGCNLAEMTILGMPIPQGFTVTTEACTEYY
NSGKQITQEIQDQIFEAITWLEELNGKKFGDTEDPLLVSVRSGARASMPG
MMDTILNLGLNDVAVEGFAKKTGNPRFAYDSYRRFIQMYSDVVMEVPKSH
FEKIIDAMKEEKGVHFDTDLTADDLKELAEKFKAVYKEAMNGEEFPQEPK
DQLMGAVKAVFRSWDNPRAIVYRRMNDIPGDWGTAVNVQTMVFGNKGETS
GTGVAFTRNPSTGEKGIYGEYLINAQGEDVVAGVRTPQPITQLENDMPDC
YKQFMDLAMKLEKHFRDMQDMEFTIEEGKLYFLQTRNGKRTAPAALQIAC
DLVDEGMITEEEAVVRIEAKSLDQLLHPTFNPAALKAGEVIGSALPASPG
AAAGKVYFTADEAKAAHEKGERVILVRLETSPEDIEGMHAAEGILTVRGG
MTSHAAVVARGMGTCCVSGCGEIKINEEAKTFELGGHTFAEGDYISLDGS
TGKIYKGDIETQEASVSGSFERIMVWADKFRTLKVRTNADTPEDTLNAVK
LGAEGIGLCRTEHMFFEADRIMKIRKMILSDSVEAREEALNELIPFQKGD
FKAMYKALEGRPMTVRYLDPPLHEFVPHTEEEQAELAKNMGLTLAEVKAK
VDELHEFNPMMGHRGCRLAVTYPEIAKMQTRAVMEAAIEVKEETGIDIVP
EIMIPLVGEKKELKFVKDVVVEVAEQVKKEKGSDMQYHIGTMIEIPRAAL
TADAIAEEAEFFSFGTNDLTQMTFGFSRDDAGKFLDSYYKAKIYESDPFA
RLDQTGVGQLVEMAVKKGRQTRPGLKCGICGEHGGDPSSVEFCHKVGLNY
VSCSPFRVPIARLAAAQAALNN
3D structure
PDB1kc7 Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K22 R92 G101 M103 R337 H455 E745 S764 D769 C831 Y851
Catalytic site (residue number reindexed from 1) K21 R91 G100 M102 R336 H454 E744 S763 D768 C830 Y850
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 MG A E745 D769 E744 D768
BS02 PPR A R561 R617 E745 G766 T767 N768 D769 R560 R616 E744 G765 T766 N767 D768 MOAD: Ki=3uM
PDBbind-CN: -logKd/Ki=5.52,Ki=3uM
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:0016310 phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1kc7, PDBe:1kc7, PDBj:1kc7
PDBsum1kc7
PubMed11790099
UniProtP22983|PPDK_CLOSY Pyruvate, phosphate dikinase (Gene Name=ppdK)

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