Structure of PDB 1glf Chain O

Receptor sequence

>1glfO (length=498) Species: 562 (Escherichia coli)

EKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPME
IWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAI
VWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGS
RERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDD
KMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALF
GQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYA
LEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGL
GAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGI
RLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAV
GFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH

3D structure

• PDB: 1glf Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
• Chain: O
• Resolution: 2.62 Å

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	PO4	O	G233 G234 R236	G232 G233 R235
BS02	ADP	O	R17 G266 T267 G310 G411 A412	R16 G265 T266 G309 G410 A411
BS03	GOL	O	R83 E84 Y135 D245	R82 E83 Y134 D244

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

External links

• PDB: RCSB:1glf, PDBe:1glf, PDBj:1glf
• PDBsum: 1glf
• PubMed: 9817843
• UniProt: P0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)