PDBsum entry: 1c81

Hydrolase

PDB id: 1c81

Contents

Protein chain

191 a.a. *

Ligands

FDQ

Waters ×249

* Residue conservation analysis

PDB id:

1c81

Name:

Hydrolase

Title:

Michaelis complex of fructose-2,6-bisphosphatase

Structure:

Fructose-2,6-bisphosphatase. Chain: a. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.209 R-free: 0.287

Authors:

Y.H.Lee,T.W.Olson,R.W.Mcclard,J.F.Witte,S.C.Mcfarlan, L.J.Banaszak,D.G.Levitt,A.J.Lange

Key ref:

Y.-H.Lee et al. Reaction mechanism of fructose-2,6-Bisphosphatase suggested by the crystal structures of a pseudo-Michaelis complex and metabolite complexes. To be published,

Date:

03-Apr-00 Release date: 10-Jun-03

Protein chain

P07953  (F261_RAT) -  6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1

Seq: 471 a.a.

Struc: 191 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 1: E.C.2.7.1.105 - 6-phosphofructo-2-kinase.
• Reaction: ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate

ATP + D-fructose 6-phosphate (Bound ligand (Het Group name = FDQ) matches with 70.00% similarity) = ADP + beta-D-fructose 2,6-bisphosphate

• Enzyme class 2: E.C.3.1.3.46 - Fructose-2,6-bisphosphate 2-phosphatase.
• Reaction: Beta-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate

Beta-D-fructose 2,6-bisphosphate + H(2)O = D-fructose 6-phosphate (Bound ligand (Het Group name = FDQ) matches with 70.00% similarity) + phosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: catalytic activity (2 terms)