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PDBsum entry 3v91

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protein ligands metals links
Transferase PDB id
3v91

 

 

 

 

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Contents
Protein chain
256 a.a.
Ligands
GOL
UPG
Metals
_CL
_MN
Waters ×93
PDB id:
3v91
Name: Transferase
Title: Structure of t82m glycogenin mutant truncated at residue 270 complexed with udp-glucose
Structure: Glycogenin-1. Chain: a. Fragment: unp residues 1-271. Synonym: gn-1, gn1. Engineered: yes. Mutation: yes
Source: Oryctolagus cuniculus. European rabbit,japanese white rabbit,domestic rabbit,rabbits. Organism_taxid: 9986. Gene: gyg, gyg1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.208     R-free:   0.236
Authors: M.E.Carrizo,J.M.Romero,F.M.Issoglio,J.A.Curtino
Key ref: M.E.Carrizo et al. (2012). Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation. Febs Lett, 586, 254-257. PubMed id: 22226635
Date:
23-Dec-11     Release date:   25-Jan-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13280  (GLYG_RABIT) -  Glycogenin-1 from Oryctolagus cuniculus
Seq:
Struc:
333 a.a.
256 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.2.4.1.186  - glycogenin glucosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L- tyrosyl-[glycogenin] + UDP + H+
2. [1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D- glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + UDP + H+
L-tyrosyl-[glycogenin]
+
UDP-alpha-D-glucose
Bound ligand (Het Group name = UPG)
corresponds exactly
= alpha-D-glucosyl-L- tyrosyl-[glycogenin]
+ UDP
+ H(+)
[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin]
+
UDP-alpha-D- glucose
Bound ligand (Het Group name = UPG)
corresponds exactly
= [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin]
+ UDP
+ H(+)
      Cofactor: Mn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Febs Lett 586:254-257 (2012)
PubMed id: 22226635  
 
 
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.
M.E.Carrizo, J.M.Romero, F.M.Issoglio, J.A.Curtino.
 
  ABSTRACT  
 
No abstract given.

 

 

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