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PDBsum entry 2kyl

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protein Protein-protein interface(s) links
Transferase PDB id
2kyl

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
96 a.a.
13 a.a.
PDB id:
2kyl
Name: Transferase
Title: Solution structure of mast2-pdz complexed with thE C-terminus of pten
Structure: Microtubule-associated serine/threonine-protein kinase 2. Chain: a. Fragment: pdz domain. Engineered: yes. C-terminus of phosphatidylinositol-3,4,5-trisphosphate 3- phosphatase and dual-specificity protein phosphatase pten. Chain: b. Synonym: c-terminus of pten. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic peptide
NMR struc: 10 models
Authors: E.Terrien,N.Wolff,F.Cordier,C.Simenel,M.Lafon,M.Delepierre
Date:
01-Jun-10     Release date:   08-Jun-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q6P0Q8  (MAST2_HUMAN) -  Microtubule-associated serine/threonine-protein kinase 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1798 a.a.
96 a.a.*
Protein chain
Pfam   ArchSchema ?
P60484  (PTEN_HUMAN) -  Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN from Homo sapiens
Seq:
Struc:
403 a.a.
13 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: Chain A: 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(+)
   Enzyme class 2: Chain B: E.C.3.1.3.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chain B: E.C.3.1.3.16  - protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
O-phospho-L-seryl-[protein]
+ H2O
= L-seryl-[protein]
+ phosphate
O-phospho-L-threonyl-[protein]
+ H2O
= L-threonyl-[protein]
+ phosphate
   Enzyme class 4: Chain B: E.C.3.1.3.48  - protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
O-phospho-L-tyrosyl-[protein]
+ H2O
= L-tyrosyl-[protein]
+ phosphate
   Enzyme class 5: Chain B: E.C.3.1.3.67  - phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- bisphosphate) + phosphate
1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate)
+ H2O
= 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- bisphosphate)
+ phosphate
      Cofactor: Mg(2+)
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

 

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