Structure of PDB 1gld Chain G

Receptor sequence

>1gldG (length=489) Species: 562 (Escherichia coli)

KYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIW
ATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVW
QCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRE
RARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKM
LEVLDIPREMLPEVRRSSEVYGQTNIIPISGIAGDQQAALFGQLCVKEGM
AKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAG
ASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA
RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDG
GAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDEL
QEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH

3D structure

• PDB: 1gld Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation.
• Chain: G
• Resolution: 2.93 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	MN	G	D10 R17	D7 R14
BS02	G3H	G	T13 R83 E84 Y135 D245 F270	T10 R80 E81 Y132 D235 F260
BS03	ADP	G	R17 G266 T267 G310 A326 G411 A412 N415	R14 G256 T257 G300 A316 G401 A402 N405

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:1gld, PDBe:1gld, PDBj:1gld
• PDBsum: 1gld
• PubMed: 8170944
• UniProt: P0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)