Structure of PDB 4d4k Chain A

Receptor sequence

>4d4kA (length=439) Species: 9606 (Homo sapiens)

PLELTQSRVQKIWVPVDHRPSLPRSNSPTVIVMVGLPARGKTYISKKLTR
YLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAAL
RDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDD
PTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCD
RDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGEN
EHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQT
AEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRY
PTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEM
PYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERS

3D structure

• PDB: 4d4k Identifying a Novel Series of Pfkfb3 Inhibitors as a Metabolic Approach to Treating Cancer from Hts, Biophysical and Biochemical Methods
• Chain: A
• Resolution: 3.24 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R252 H253 N259 S302 E322 H387
• Catalytic site (residue number reindexed from 1): R246 H247 N253 S296 E316 H381
• Enzyme Commision number: 2.7.1.105: 6-phosphofructo-2-kinase.
  3.1.3.46: fructose-2,6-bisphosphate 2-phosphatase.

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	PHS	A	R252 H253 N259 H387 Q388	R246 H247 N253 H381 Q382
BS02	F6P	A	E322 Y333 R347 K351 Y362 Q388 R392	E316 Y327 R341 K345 Y356 Q382 R386
BS03	BKE	A	R45 G46 Y49 I50 V159 N163 E166 V214 V217 A423	R39 G40 Y43 I44 V153 N157 E160 V208 V211 A417

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003873 6-phosphofructo-2-kinase activity
• GO:0005524 ATP binding

Biological Process

• GO:0006000 fructose metabolic process
• GO:0006003 fructose 2,6-bisphosphate metabolic process

External links

• PDB: RCSB:4d4k, PDBe:4d4k, PDBj:4d4k
• PDBsum: 4d4k
• UniProt: Q16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)