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PDBsum entry 2vkn

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protein ligands links
Membrane protein PDB id
2vkn

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
66 a.a. *
Ligands
LYS-PRO-LEU-PRO-
PRO-LEU-PRO-LEU-
ALA
SO4 ×3
Waters ×37
* Residue conservation analysis
PDB id:
2vkn
Name: Membrane protein
Title: Yeast sho1 sh3 domain complexed with a peptide from pbs2
Structure: Protein ssu81. Chain: a. Fragment: sh3 domain, residues 298-367. Synonym: sho1 osmosensor, sho1. Engineered: yes. Map kinase kinase pbs2. Chain: c. Fragment: proline-rich domain, residues 2-13. Synonym: polymyxin b resistance protein 2, suppressor of fluoride
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 4932
Resolution:
2.05Å     R-factor:   0.171     R-free:   0.238
Authors: P.Kursula,I.Kursula,Y.H.Song,K.Paraskevopoulos,M.Wilmanns
Key ref: P.Kursula et al. Structural genomics of yeast sh3 domains. To be published, .
Date:
20-Dec-07     Release date:   05-Feb-08    
Supersedes: 2qk6
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P40073  (SHO1_YEAST) -  High osmolarity signaling protein SHO1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
367 a.a.
66 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.12.2  - mitogen-activated protein kinase 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+
3. L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
L-tyrosyl-[protein]
+ ATP
= O-phospho-L-tyrosyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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