1gpa Summary

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STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP

The structure was published by Barford, D., Hu, S.H., and Johnson, L.N., in 1991 in a paper entitled "Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 1990.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of GLYCOGEN PHOSPHORYLASE A.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A GLYCOGEN PHOSPHORYLASE A P00489 (2-843) (PYGM_RABIT)search Oryctolagus cuniculussearch 98% 842 98%
B GLYCOGEN PHOSPHORYLASE A P00489 (2-843) (PYGM_RABIT)search Oryctolagus cuniculussearch 98% 842 98%
C GLYCOGEN PHOSPHORYLASE A P00489 (2-843) (PYGM_RABIT)search Oryctolagus cuniculussearch 98% 842 98%
D GLYCOGEN PHOSPHORYLASE A P00489 (2-843) (PYGM_RABIT)search Oryctolagus cuniculussearch 98% 842 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00489 (2 - 843) GLYCOGEN PHOSPHORYLASE A Oryctolagus cuniculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P00489) Oligosaccharide phosphorylasesearch Glycogen Phosphorylase B;search PF00343: Carbohydrate phosphorylasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D (P00489) phosphorylase activitysearch catalytic activitysearch transferase activity, transferring glycosyl groupssearch glycogen phosphorylase activitysearch nucleotide bindingsearch transferase activitysearch pyridoxal phosphate bindingsearch glycogen metabolic processsearch carbohydrate metabolic processsearch metabolic processsearch glycogen catabolic processsearch

Chain InterPro annotation
A, B, C, D Glycosyl transferase, family 35search Glycogen/starch/alpha-glucan phosphorylasesearch