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protein ligands Protein-protein interface(s) links
Transferase PDB id
2c4m
Jmol
Contents
Protein chains
789 a.a. *
Ligands
PLP ×4
PO4 ×9
FMT ×19
EDO ×3
Waters ×1154
* Residue conservation analysis
PDB id:
2c4m
Name: Transferase
Title: Starch phosphorylase: structural studies explain oxyanion- dependent kinetic stability and regulatory control.
Structure: Glycogen phosphorylase. Chain: a, b, c, d. Synonym: starch phosphorylase. Engineered: yes. Mutation: yes. Other_details: plp (1634) cofactor is covalently linked to lys634 via schiff base (c4a-nz)
Source: Corynebacterium callunae. Organism_taxid: 1721. Atcc: dsm 20145. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: xl1 blue.
Resolution:
1.90Å     R-factor:   0.216     R-free:   0.232
Authors: A.Purvis,B.Nidetzky,K.Watson
Key ref: A.Purvis et al. Starch phosphorylase: structural studies explain oxyanion-Dependent kinetic stability and regulatory control. To be published,
Date:
20-Oct-05     Release date:   27-Feb-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8KQ56  (Q8KQ56_9CORY) -  Phosphorylase
Seq:
Struc:
 
Seq:
Struc:
796 a.a.
789 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.4.1.1  - Phosphorylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Glycogen
      Reaction: (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate
(1,4-alpha-D-glucosyl)(n)
+
phosphate
Bound ligand (Het Group name = PO4)
corresponds exactly
= (1,4-alpha-D-glucosyl)(n-1)
+
alpha-D-glucose 1-phosphate
Bound ligand (Het Group name = PLP)
matches with 63.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     transferase activity     4 terms