Structure of PDB 2dwp Chain A

Receptor sequence
>2dwpA (length=431) Species: 9606 (Homo sapiens) [Search protein sequence]
ELTQSRVQKIWVPVDHRNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVP
TKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLA
KEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNI
MEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKV
IDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRI
GGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPY
EQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQD
LVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLH
TVLKLTPVAYGCRVESIYLNVESVCTHRERS
3D structure
PDB2dwp A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R252 H253 N259 S302 E322 H387
Catalytic site (residue number reindexed from 1) R238 H239 N245 S288 E308 H373
Enzyme Commision number 2.7.1.105: 6-phosphofructo-2-kinase.
3.1.3.46: fructose-2,6-bisphosphate 2-phosphatase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003873 6-phosphofructo-2-kinase activity
GO:0004331 fructose-2,6-bisphosphate 2-phosphatase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006000 fructose metabolic process
GO:0006003 fructose 2,6-bisphosphate metabolic process
GO:0006096 glycolytic process
GO:0006915 apoptotic process
GO:0010001 glial cell differentiation
GO:0016310 phosphorylation
GO:0046835 carbohydrate phosphorylation
GO:0061744 motor behavior
Cellular Component
GO:0005654 nucleoplasm
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:2dwp, PDBe:2dwp, PDBj:2dwp
PDBsum2dwp
PubMed17499765
UniProtQ16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)

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