Structure of PDB 2dwo Chain A

Receptor sequence
>2dwoA (length=449) Species: 9606 (Homo sapiens) [Search protein sequence]
LELTQSRVQKIWVPVDHRPSLPRSCGPNSPTVIVMVGLPARGKTYISKKL
TRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALA
ALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVC
DDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDK
CDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHG
ENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTI
QTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYY
RYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAE
EMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSNPLMRRNS
3D structure
PDB2dwo A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase
ChainA
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) R252 H253 N259 S302 E322 H387
Catalytic site (residue number reindexed from 1) R248 H249 N255 S298 E318 H383
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:2dwo, PDBe:2dwo, PDBj:2dwo
PDBsum2dwo
PubMed17499765
UniProtQ16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)

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