Structure of PDB 1bu6 Chain O

Receptor sequence
>1bu6O (length=497) Species: 562 (Escherichia coli) [Search protein sequence]
KKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEI
WATQSSTLVEVLTKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIV
WQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSR
ERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDK
MLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFG
QLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYAL
EGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLG
APYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIR
LHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVG
FWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH
3D structure
PDB1bu6 Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
ChainO
Resolution2.37 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.30: glycerol kinase.
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 GOL O R83 E84 W103 Y135 D245 R81 E82 W101 Y133 D243
Gene Ontology
Molecular Function
GO:0004370 glycerol kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006071 glycerol metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0019563 glycerol catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1bu6, PDBe:1bu6, PDBj:1bu6
PDBsum1bu6
PubMed9817843
UniProtP0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)

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