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PDBsum entry 4xhg

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protein ligands links
Transferase PDB id
4xhg

 

 

 

 

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Contents
Protein chain
357 a.a.
Ligands
ADP
FMT
Waters ×285
PDB id:
4xhg
Name: Transferase
Title: Structure of c. Glabrata hrr25 bound to adp (formate condition)
Structure: Similar to uniprot|p29295 saccharomyces cerevisiae ypl204w hrr25. Chain: a. Fragment: unp residues 1-403. Engineered: yes. Mutation: yes
Source: Candida glabrata. Organism_taxid: 5478. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.15Å     R-factor:   0.176     R-free:   0.216
Authors: Q.Ye,K.D.Corbett
Key ref: Q.Ye et al. (2016). Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. Embo J, 35, 2139-2151. PubMed id: 27491543 DOI: 10.15252/embj.201694082
Date:
05-Jan-15     Release date:   06-Jan-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q6FS46  (Q6FS46_CANGA) -  Candida glabrata strain CBS138 chromosome H complete sequence from Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138)
Seq:
Struc:
495 a.a.
357 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
Bound ligand (Het Group name = ADP)
corresponds exactly
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name = ADP)
corresponds exactly
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.15252/embj.201694082 Embo J 35:2139-2151 (2016)
PubMed id: 27491543  
 
 
Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator.
Q.Ye, S.N.Ur, T.Y.Su, K.D.Corbett.
 
  ABSTRACT  
 
No abstract given.

 

 

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