Structure of PDB 4d4m Chain A

Receptor sequence

>4d4mA (length=439) Species: 9606 (Homo sapiens)

PLELTQSRVQKIWVPVDHRPSLPRSCNSPTVIVMVGLPARGKTYISKKLT
RYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAA
LRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCD
DPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKC
DRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGE
NEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQ
TAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYR
YPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEE
MPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRER

3D structure

• PDB: 4d4m Identifying a Novel Series of Pfkfb3 Inhibitors as a Metabolic Approach to Treating Cancer from Hts, Biophysical and Biochemical Methods
• Chain: A
• Resolution: 2.32 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R252 H253 N259 S302 E322 H387
• Catalytic site (residue number reindexed from 1): R247 H248 N254 S297 E317 H382
• 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	R247 H248 N254 H382 Q383
BS02	F6P	A	G265 E322 Y333 R347 K351 Y362 Q388 R392	G260 E317 Y328 R342 K346 Y357 Q383 R387
BS03	BKV	A	R45 G46 Y49 I50 V159 N163 E166 V214 V217 L238 I241 V243	R40 G41 Y44 I45 V154 N158 E161 V209 V212 L233 I236 V238

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:4d4m, PDBe:4d4m, PDBj:4d4m
• PDBsum: 4d4m
• UniProt: Q16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)