Structure of PDB 4d4j Chain A

Receptor sequence

>4d4jA (length=442) Species: 9606 (Homo sapiens)

PLELTQSRVQKIWVPVDHRPSLPRSCGPNSPTVIVMVGLPARGKTYISKK
LTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCAL
AALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESV
CDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPD
KCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRH
GENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKST
IQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYY
YRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSA
EEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERS

3D structure

• PDB: 4d4j Identifying a Novel Series of Pfkfb3 Inhibitors as a Metabolic Approach to Treating Cancer from Hts, Biophysical and Biochemical Methods
• Chain: A
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R252 H253 N259 S302 E322 H387
• Catalytic site (residue number reindexed from 1): R249 H250 N256 S299 E319 H384
• 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 E322 H387 Q388	R249 H250 E319 H384 Q385
BS02	F6P	A	I264 G265 E322 Y333 R347 K351 Y362 Q388 R392	I261 G262 E319 Y330 R344 K348 Y359 Q385 R389
BS03	BKI	A	R45 G46 Y49 I50 V159 N163 E166 V214 V217 L238 I241 V243	R42 G43 Y46 I47 V156 N160 E163 V211 V214 L235 I238 V240

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:4d4j, PDBe:4d4j, PDBj:4d4j
• PDBsum: 4d4j
• UniProt: Q16875|F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (Gene Name=PFKFB3)