Brand  (β version)

PDB ID: 1ABB

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
IMP Inosinic acid PoSSuM
PDP Pyridoxal-5'-diphosphate PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1ABB   PDBj   RCSB PDB   PDBe
Header : GLYCOGEN PHOSPHORYLASE
Title : CONTROL OF PHOSPHORYLASE B CONFORMATION BY A MODIFIED COFACTOR: CRYSTALLOGRAPHIC STUDIES ON R-STATE GLYCOGEN PHOSPHORYLASE RECONSTITUTED WITH PYRIDOXAL 5'-DIPHOSPHATE
Release Data : 1993-10-31
Compound :
mol_id molecule chains
1 GLYCOGEN PHOSPHORYLASE B A,B,C,D
ec: 2.4.1.1
Source :
mol_id organism_scientific organism_common
1 Oryctolagus cuniculus  (taxid:9986) Rabbit
Authors : Leonidas, D.D., Oikonomakos, N.G., Papageorgiou, A.C., Acharya, K.R., Barford, D., Johnson, L.N.
Keywords : GLYCOGEN PHOSPHORYLASE
Exp. method : X-RAY DIFFRACTION ( 2.8 Å )
Citation :

Control of phosphorylase b conformation by a modified cofactor: crystallographic studies on R-state glycogen phosphorylase reconstituted with pyridoxal 5'-diphosphate.

Leonidas, D.D.,Oikonomakos, N.G.,Papageorgiou, A.C.  et al.
(1992)  Protein Sci.  1 : 1112 - 1122

PubMed: 1304390

The Allosteric Transition of Glycogen Phosphorylase

Barford, D.,Johnson, L.N.
(1989)  Nature  340 : 609

Reaction

Chain : A, B, C, D
UniProt : P00489 (PYGM_RABIT)
Reaction: EC: Evidence:
Physiological Direction:
[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- glucosyl](n-1) + alpha-D-glucose 1-phosphate 2.4.1.1 UniProtKB:P11217
left-to-right