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PDBsum entry 1yr5

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protein metals Protein-protein interface(s) links
Metal binding protein/transferase PDB id
1yr5

 

 

 

 

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Contents
Protein chains
146 a.a. *
19 a.a. *
Metals
_CA ×4
Waters ×144
* Residue conservation analysis
PDB id:
1yr5
Name: Metal binding protein/transferase
Title: 1.7-a structure of calmodulin bound to a peptide from dap kinase
Structure: Calmodulin. Chain: a. Fragment: residues 1-148. Engineered: yes. 19-mer from death-associated protein kinase 1. Chain: b. Synonym: dap kinase 1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic peptide
Biol. unit: Tetramer (from PQS)
Resolution:
1.70Å     R-factor:   0.203     R-free:   0.257
Authors: P.Kursula,J.Vahokoski,M.Wilmanns
Key ref: P.Kursula et al. Recognition of human death-Associated protein kinases by calmodulin. To be published, .
Date:
03-Feb-05     Release date:   04-Jul-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens
Seq:
Struc:
149 a.a.
146 a.a.
Protein chain
Pfam   ArchSchema ?
P53355  (DAPK1_HUMAN) -  Death-associated protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1430 a.a.
19 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: 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(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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