PDBsum entry: 2c4m

Transferase

PDB-id: 2c4m

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Description

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References

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Protein chains

789 a.a. *

Ligands

PLP ×4

PO4 ×9

FMT ×19

EDO ×3

Waters ×1154

* Residue conservation analysis

Tools

Clefts Calculation

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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)

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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