Brand  (β version)

PDB ID: 1L5Q

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Ligands
Code Name Style Show Link
PLP Pyridoxal-5'-phosphate PoSSuM
700 [5-chloro-1h-indol-2-carbonyl-phenylalaninyl]-azetidine-3-carboxylic acid PoSSuM
CFF Caffeine PoSSuM
NBG N-acetyl-beta-D-glucopyranosylamine PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1L5Q   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Human liver glycogen phosphorylase a complexed with caffeine, N-Acetyl-beta-D-glucopyranosylamine, and CP-403700
Release Data : 2002-12-04
Compound :
mol_id molecule chains synonym
1 Glycogen phosphorylase, liver form A,B Glycogen phosphorylase A
ec: 2.4.1.1
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
organ: liver
Authors : Ekstrom, J.L., Pauly, T.A., Carty, M.D., Soeller, W.C., Culp, J., Danley, D.E., Hoover, D.J., Treadway, J.L., Gibbs, E.M., Fletterick, R.J., Day, Y.S.N., Myszka, D.G., Rath, V.L.
Keywords : phosphorylase, purine site, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.25 Å )
Citation :

Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase.

Ekstrom, J.L.,Pauly, T.A.,Carty, M.D.  et al.
(2002)  Chem.Biol.  9 : 915 - 924

PubMed: 12204691
DOI: 10.1016/S1074-5521(02)00186-2

Reaction

Chain : A, B
UniProt : P06737 (PYGL_HUMAN)
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 PubMed:22225877
left-to-right
Cofactor: Evidence: Note:
pyridoxal 5'-phosphate ECO:0000269 | PubMed:10949035
ECO:0000269 | PubMed:10980448
ECO:0000269 | PubMed:12204691
ECO:0007744 | PDB:1EM6
ECO:0007744 | PDB:1EXV
ECO:0007744 | PDB:1FA9
ECO:0007744 | PDB:1FC0
ECO:0007744 | PDB:1L5Q
ECO:0007744 | PDB:1L5R
ECO:0007744 | PDB:1L5S
ECO:0007744 | PDB:1L7X
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