Structure of PDB 1rk2 Chain D

Receptor sequence
>1rk2D (length=305) Species: 562 (Escherichia coli) [Search protein sequence]
AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGR
SGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVN
GEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAA
KIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAA
GDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDA
FLDRQ
3D structure
PDB1rk2 Induced fit on sugar binding activates ribokinase.
ChainD
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 RIB D N14 D16 G41 G42 K43 N46 A98 E143 D255 N11 D13 G38 G39 K40 N43 A95 E140 D252
BS02 ALF D G216 R218 G213 R215
BS03 MG D D249 A285 V286 R288 S294 D246 A282 V283 R285 S291
BS04 ADP D N187 T223 G225 S226 G254 H279 A282 N184 T220 G222 S223 G251 H276 A279
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

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Cellular Component
External links
PDB RCSB:1rk2, PDBe:1rk2, PDBj:1rk2
PDBsum1rk2
PubMed10438599
UniProtP0A9J6|RBSK_ECOLI Ribokinase (Gene Name=rbsK)

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