Structure of PDB 1rkd Chain A

Receptor sequence
>1rkdA (length=306) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGR
SGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVN
GEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAA
KIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAA
GDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDA
FLDRQR
3D structure
PDB1rkd 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.
ChainA
Resolution1.84 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 A N14 D16 G42 K43 N46 A98 E143 D255 N11 D13 G39 K40 N43 A95 E140 D252
BS02 ADP A T223 G225 G254 H279 A282 T220 G222 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rkd, PDBe:1rkd, PDBj:1rkd
PDBsum1rkd
PubMed9519409
UniProtP0A9J6|RBSK_ECOLI Ribokinase (Gene Name=rbsK)

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