Structure of PDB 4lrz Chain B

Receptor sequence
>4lrzB (length=211) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GSSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKV
VEKLPAIADKDIGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQ
SLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNL
SVPVALEAASSIAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMF
MMQMLALAAKE
3D structure
PDB4lrz Coiled-Coil Helix Rotation Selects Repressing or Activating State of Transcriptional Regulator DhaR.
ChainB
Resolution2.32 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 ADP B D30 D35 D37 H38 G78 A79 S80 L83 G121 T129 M130 R178 D191 P192 G193 D31 D36 D38 H39 G79 A80 S81 L84 G122 T130 M131 R179 D192 P193 G194
BS02 MG B D30 D35 D37 D31 D36 D38
BS03 MG B D35 D37 D36 D38
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004371 glycerone kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016740 transferase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0043531 ADP binding
GO:0046872 metal ion binding
GO:0047324 phosphoenolpyruvate-glycerone phosphotransferase activity
Biological Process
GO:0006071 glycerol metabolic process
GO:0006090 pyruvate metabolic process
GO:0016310 phosphorylation
GO:0019563 glycerol catabolic process
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1990234 transferase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:4lrz, PDBe:4lrz, PDBj:4lrz
PDBsum4lrz
PubMed24440518
UniProtP76014|DHAL_ECOLI PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL (Gene Name=dhaL)

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