Structure of PDB 1gqt Chain A

Receptor sequence

>1gqtA (length=305) Species: 83333 (Escherichia coli K-12)

AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGR
SGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVN
GEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAA
KIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAA
GDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDA
FLDRQ

3D structure

• PDB: 1gqt Activation of Ribokinase by Monovalent Cations.
• Chain: A
• Resolution: 2.34 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A252 A253 G254 D255
• Catalytic site (residue number reindexed from 1): A249 A250 G251 D252
• Enzyme Commision number: 2.7.1.15: ribokinase.

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	CS	A	D249 I251 A285 R288 G290 S294	D246 I248 A282 R285 G287 S291
BS02	ACP	A	N187 T223 G225 V245 A252 G254 D255 H279 A282	N184 T220 G222 V242 A249 G251 D252 H276 A279
BS03	RIB	A	N14 D16 G41 G42 N46 A98 E143 D255	N11 D13 G38 G39 N43 A95 E140 D252

Gene Ontology

Molecular Function

• GO:0004747 ribokinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006014 D-ribose metabolic process
• GO:0016310 phosphorylation
• GO:0019303 D-ribose catabolic process
• GO:0046835 carbohydrate phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1gqt, PDBe:1gqt, PDBj:1gqt
• PDBsum: 1gqt
• PubMed: 11786021
• UniProt: P0A9J6|RBSK_ECOLI Ribokinase (Gene Name=rbsK)