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PDBsum entry 2x1l

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protein ligands Protein-protein interface(s) links
Ligase PDB id
2x1l
Jmol PyMol
Contents
Protein chains
511 a.a. *
474 a.a. *
Ligands
MET ×3
ADN ×3
CXS ×3
2HP ×3
Waters ×484
* Residue conservation analysis
PDB id:
2x1l
Name: Ligase
Title: Crystal structure of mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine and adenosine
Structure: Methionyl-tRNA synthetase. Chain: a, b, c. Fragment: residues 2-515. Engineered: yes
Source: Mycobacterium smegmatis. Organism_taxid: 246196. Strain: mc2 155. Atcc: 700084. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.30Å     R-factor:   0.219     R-free:   0.249
Authors: H.Ingvarsson,T.A.Jones,T.Unge
Key ref: H.Ingvarsson and T.Unge (2010). Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase. FEBS J, 277, 3947-3962. PubMed id: 20796028
Date:
31-Dec-09     Release date:   28-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0R3E2  (A0R3E2_MYCS2) -  Methionine--tRNA ligase
Seq:
Struc:
515 a.a.
511 a.a.
Protein chains
Pfam   ArchSchema ?
A0R3E2  (A0R3E2_MYCS2) -  Methionine--tRNA ligase
Seq:
Struc:
515 a.a.
474 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C: E.C.6.1.1.10  - Methionine--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl- tRNA(Met)
ATP
+
L-methionine
Bound ligand (Het Group name = MET)
corresponds exactly
+ tRNA(Met)
=
AMP
Bound ligand (Het Group name = ADN)
matches with 82.00% similarity
+
diphosphate
Bound ligand (Het Group name = 2HP)
matches with 55.00% similarity
+ L-methionyl- tRNA(Met)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     translation   3 terms 
  Biochemical function     nucleotide binding     5 terms  

 

 
    reference    
 
 
FEBS J 277:3947-3962 (2010)
PubMed id: 20796028  
 
 
Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase.
H.Ingvarsson, T.Unge.
 
  ABSTRACT  
 
No abstract given.

 

 

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