Structure of PDB 1rk2 Chain A Binding Site BS02
Receptor Information
>1rk2 Chain A (length=305) Species:
562
(Escherichia coli) [
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AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGR
SGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVN
GEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAA
KIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAA
GDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDA
FLDRQ
Ligand information
Ligand ID
ALF
InChI
InChI=1S/Al.4FH/h;4*1H/q+3;;;;/p-4
InChIKey
UYOMQIYKOOHAMK-UHFFFAOYSA-J
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
F[Al-](F)(F)F
Formula
Al F4
Name
TETRAFLUOROALUMINATE ION
ChEMBL
DrugBank
DB04444
ZINC
PDB chain
1rk2 Chain A Residue 315 [
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Receptor-Ligand Complex Structure
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PDB
1rk2
Induced fit on sugar binding activates ribokinase.
Resolution
2.25 Å
Binding residue
(original residue number in PDB)
G216 R218
Binding residue
(residue number reindexed from 1)
G213 R215
Annotation score
1
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.
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:1rk2
,
PDBe:1rk2
,
PDBj:1rk2
PDBsum
1rk2
PubMed
10438599
UniProt
P0A9J6
|RBSK_ECOLI Ribokinase (Gene Name=rbsK)
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