Structure of PDB 1bo5 Chain O

Receptor sequence
>1bo5O (length=498) Species: 562 (Escherichia coli) [Search protein sequence]
EKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPME
IWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAI
VWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGS
RERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDD
KMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALF
GQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYA
LEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGL
GAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGI
RLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAV
GFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH
3D structure
PDB1bo5 Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate.
ChainO
Resolution3.2 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 FBP O G233 G234 R236 G232 G233 R235 PDBbind-CN: -logKd/Ki=3.60,Ki=0.25mM
BS02 GOL O R83 E84 W103 Y135 D245 Q246 F270 R82 E83 W102 Y134 D244 Q245 F269
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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Biological Process
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Cellular Component
External links
PDB RCSB:1bo5, PDBe:1bo5, PDBj:1bo5
PDBsum1bo5
PubMed9843423
UniProtP0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)

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