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PDBsum entry 1pg8

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protein ligands Protein-protein interface(s) links
Lyase PDB id
1pg8

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
398 a.a. *
Ligands
SO4 ×4
PLP ×4
PEG ×11
Waters ×424
* Residue conservation analysis
PDB id:
1pg8
Name: Lyase
Title: Crystal structure of l-methionine alpha-, gamma-lyase
Structure: Methionine gamma-lyase. Chain: a, b, c, d. Synonym: l-methioninase. Ec: 4.4.1.11
Source: Pseudomonas putida. Organism_taxid: 303
Biol. unit: Octamer (from PQS)
Resolution:
2.68Å     R-factor:   0.182     R-free:   0.236
Authors: T.W.Allen,V.Sridhar,G.S.Prasad,Q.Han,M.Xu,Y.Tan,R.M.Hoffman, S.Ramaswamy
Date:
28-May-03     Release date:   08-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P13254  (MEGL_PSEPU) -  L-methionine gamma-lyase from Pseudomonas putida
Seq:
Struc:
398 a.a.
398 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.4.4.1.11  - methionine gamma-lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-methionine + H2O = methanethiol + 2-oxobutanoate + NH4+
L-methionine
+ H2O
=
methanethiol
Bound ligand (Het Group name = PEG)
matches with 40.00% similarity
+ 2-oxobutanoate
+ NH4(+)
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
   Enzyme class 2: E.C.4.4.1.2  - homocysteine desulfhydrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-homocysteine + H2O = 2-oxobutanoate + hydrogen sulfide + NH4+ + H+
L-homocysteine
+ H2O
=
2-oxobutanoate
Bound ligand (Het Group name = PEG)
matches with 40.00% similarity
+ hydrogen sulfide
+ NH4(+)
+ H(+)
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
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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