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Transferase PDB-id
2c4m
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Description
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Protein chains
789 a.a. *
Ligands
PLP ×4
PO4 ×9
FMT ×19
EDO ×3
Waters ×1154

* Residue conservation analysis
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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.

UniProt:
Chains A, B, C, D: Q8KQ56 (Q8KQ56_9CORY)
Pfam  
Seq:
Struc:
Seq:
Struc:
Seq:
Struc:
Seq: 796 a.a.
Struc: 789 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

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

Reaction:
(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate (see diagram below)

Pathway:
Glycogen

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, xsi:nil="true" />.

Date:
20-Oct-05

Release date:
27-Feb-07
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Enzyme reaction for E.C.2.4.1.1

{(1,4)-alpha-D-glucosyl}(N)
+
phosphate
= {(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.