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PDBsum entry 3fe3

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protein Protein-protein interface(s) links
Transferase PDB id
3fe3

 

 

 

 

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Contents
Protein chains
317 a.a. *
Waters ×398
* Residue conservation analysis
PDB id:
3fe3
Name: Transferase
Title: Crystal structure of the kinase mark3/par-1: t211a-s215a double mutant
Structure: Map/microtubule affinity-regulating kinase 3. Chain: a, b. Fragment: catalytic and ubiquitin-associated domains, unp residues 41-367. Synonym: cdc25c-associated protein kinase 1, c-tak1, ctak1, serine/threonine protein kinase p78, ser/thr protein kinase par-1, protein kinase stk10. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mark3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.199     R-free:   0.233
Authors: C.Nugoor,A.Marx,S.Panneerselvam,E.-M.Mandelkow,E.Mandelkow
Key ref: C.Nugoor et al. Crystal structure of the kinase mark3/par-1: t211a-S215a double mutant. To be published, .
Date:
27-Nov-08     Release date:   16-Dec-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27448  (MARK3_HUMAN) -  MAP/microtubule affinity-regulating kinase 3 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
753 a.a.
317 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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]
+ 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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