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PDBsum entry 2lcs

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protein Protein-protein interface(s) links
Transferase, signaling protein PDB id
2lcs

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
67 a.a.
16 a.a.
PDB id:
2lcs
Name: Transferase, signaling protein
Title: Yeast nbp2p sh3 domain in complex with a peptide from ste20p
Structure: Nap1-binding protein 2. Chain: a. Fragment: sh3 domain residues 110-172. Engineered: yes. Serine/threonine-protein kinase ste20. Chain: b. Fragment: sequence database residues 468-483. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: nbp2, ydr162c. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Saccharomyces cerevisiae s288c.
NMR struc: 20 models
Authors: M.Gorelik,A.R.Davidson
Key ref: M.Gorelik and A.R.Davidson (2012). Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface. J Biol Chem, 287, 9168-9177. PubMed id: 22277653
Date:
07-May-11     Release date:   01-Feb-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q12163  (NBP2_YEAST) -  NAP1-binding protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
236 a.a.
67 a.a.*
Protein chain
Pfam   ArchSchema ?
Q03497  (STE20_YEAST) -  Serine/threonine-protein kinase STE20 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
939 a.a.
16 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: Chain A: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chain B: 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]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 287:9168-9177 (2012)
PubMed id: 22277653  
 
 
Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface.
M.Gorelik, A.R.Davidson.
 
  ABSTRACT  
 
No abstract given.

 

 

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