Brand  (β version)

PDB ID: 2I1V

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
ADP Adenosine-5'-diphosphate PoSSuM
PHS Phosphonic acid PoSSuM
F6P 6-O-phosphono-beta-D-fructofuranose PoSSuM
FDP 2,6-di-O-phosphono-beta-D-fructofuranose PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 2I1V   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE, HYDROLASE
Title : Crystal structure of PFKFB3 in complex with ADP and Fructose-2,6-bisphosphate
Release Data : 2007-07-03
Compound :
mol_id molecule chains synonym
1 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 B PFKFB3, Phosphoryl transferase
ec: 2.7.1.105, 3.1.3.46
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
Authors : Kim, S.G., El-Maghrabi, M.R., Lee, Y.H.
Keywords : ternary product complex, ADP and F-2, 6-P2 in 2-Kase, E-P and F-6-P in 2-Pase, TRANSFERASE, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase

Kim, S.G.,Cavalier, M.,El-Maghrabi, M.R.  et al.
(2007)  J.Mol.Biol.  370 : 14 - 26

PubMed: 17499765
DOI: 10.1016/j.jmb.2007.03.038

Reaction

Chain : B
UniProt : Q16875 (F263_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6- phosphate + phosphate 3.1.3.46 PubMed:16316985, PubMed:17499765, PubMed:22275052
left-to-right PubMed:16316985
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6- bisphosphate + H(+) 2.7.1.105 PubMed:10077634, PubMed:17499765, PubMed:16316985
left-to-right PubMed:10077634