Brand  (β version)

PDB ID: 1GQT

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Ligands
Code Name Style Show Link
CS Cesium ion PoSSuM
ACP Phosphomethylphosphonic acid adenylate ester PoSSuM
RIB Alpha-D-ribofuranose PoSSuM
Non-standard Residues
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Structure summary

Code : 1GQT   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Activation of Ribokinase by Monovalent Cations
Release Data : 2002-01-28
Compound :
mol_id molecule chains
1 RIBOKINASE A,B,C,D
ec: 2.7.1.15
Source :
mol_id organism_scientific expression_system
1 ESCHERICHIA COLI  (taxid:83333) ESCHERICHIA COLI  (taxid:562)
strain: K12
expression_system_strain: MRI240
expression_system_plasmid: PJGK10
Authors : Andersson, C.E., Mowbray, S.L.
Keywords : CARBOHYDRATE KINASE, RIBOSE, TRANSFERASE, INDUCED FIT, BINDING OF MONOVALENT CATIONS, ACTIVATION BY MONOVALENT CATIONS
Exp. method : X-RAY DIFFRACTION ( 2.34 Å )
Citation :

Activation of Ribokinase by Monovalent Cations.

Andersson, C.E.,Mowbray, S.L.
(2002)  J.Mol.Biol.  315 : 409

PubMed: 11786021
DOI: 10.1006/JMBI.2001.5248

Structure of Escherichia Coli Ribokinase in Complex with Ribose and Dinucleotide Determined to 1.8 A Resolution: Insights Into a New Family of Kinase Structures.

Sigrell, J.A.,Cameron, A.D.,Jones, T.A.  et al.
(1998)  Structure  6 : 183

PubMed: 9519409
DOI: 10.1016/S0969-2126(98)00020-3

Ribokinase from Escherichia Coli K12. Nucleotide Sequence and Overexpression of the Rbsk Gene and Purification of Ribokinase

Hope, J.N.,Bell, A.W.,Hermodson, M.A.  et al.
(1986)  J.Biol.Chem.  261 : 7663

PubMed: 3011794

Induced fit on sugar binding activates ribokinase.

Sigrell, J.A.,Cameron, A.D.,Mowbray, S.L.
(1999)  J. Mol. Biol.  290 : 1009 - 1018

PubMed: 10438599
DOI: 10.1006/jmbi.1999.2938

Reaction

Chain : A, B, C, D
UniProt : P05054 (RBSK_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
D-ribose + ATP = D-ribose 5-phosphate + ADP + H(+) 2.7.1.15 HAMAP-Rule:MF_01987, PubMed:11563694, PubMed:16784868, PubMed:3011794
-
Cofactor: Evidence: Note:
Mn(2+) ECO:0000255 | HAMAP-Rule:MF_01987
ECO:0000269 | PubMed:16784868
ECO:0000305 | PubMed:11786021
ECO:0000269 | PubMed:16784868
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate (Probable). Also active with manganase (PubMed:16784868).