Structure of PDB 3pnq Chain D

Receptor sequence
>3pnqD (length=334) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
DVLDEQLAGLAKAHPSLTLHQDPVYVTRADAPVAGKVALLSGGGSGNEPM
HCGYIGQGMLSGACPGEIFTSPTPDKIFECAMQVDGGEGVLLIIKNYTGD
ILNFETATELLHDSGVKVTTVVIDDDVAVKDSLYTAGRRGVANTVLIEKL
VGAAAERGDSLDACAELGRKLNNQGHSIGIALGLADNEMEFGVGIHGEPG
IDRRPFSSLDQTVDEMFDTLLVNGSYHRTLRFWDYQQGSWQEEQQTKQPL
QSGDRVIALVNNLGATPLSELYGVYNRLTTRCQQAGLTIERNLIGAYCTS
LDMTGFSITLLKVDDETLALWDAPVHTPALNWGK
3D structure
PDB3pnq Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.
ChainD
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.121: phosphoenolpyruvate--glycerone phosphotransferase.
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 2HA D G52 G53 S80 K104 Y106 D109 H218 G43 G44 S71 K95 Y97 D100 H196
Gene Ontology
Molecular Function
GO:0004371 glycerone kinase activity
GO:0005515 protein binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0047324 phosphoenolpyruvate-glycerone phosphotransferase activity
Biological Process
GO:0006071 glycerol metabolic process
GO:0006090 pyruvate metabolic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0019563 glycerol catabolic process
GO:0042182 ketone catabolic process
GO:0046365 monosaccharide catabolic process
GO:0046835 carbohydrate phosphorylation
GO:0061610 glycerol to glycerone phosphate metabolic process
Cellular Component
GO:0005829 cytosol
GO:1990234 transferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3pnq, PDBe:3pnq, PDBj:3pnq
PDBsum3pnq
PubMed21209328
UniProtP76015|DHAK_ECOLI PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK (Gene Name=dhaK)

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