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PDBsum entry 7nu1

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protein metals links
Ligase PDB id
7nu1

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
805 a.a.
Metals
_MG
_ZN
Waters ×115
PDB id:
7nu1
Name: Ligase
Title: Crystal structure of neisseria gonorrhoeae leurs e169g mutant
Structure: Leucine--tRNA ligase. Chain: a. Fragment: leucyl-tRNA synthetase. Synonym: leucyl-tRNA synthetase,leurs. Engineered: yes. Mutation: yes
Source: Neisseria gonorrhoeae. Organism_taxid: 485. Strain: nccp11945. Gene: leus, ngk_0009. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.51Å     R-factor:   0.206     R-free:   0.262
Authors: L.Pang,S.V.Strelkov,S.D.Weeks
Key ref: L.Pang et al. Partitioning of the initial catalytic steps of leucyl synthetase is driven by an active site peptide-Plane. Commun biol, . PubMed id: 36038645
Date:
11-Mar-21     Release date:   31-Aug-22    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
B4RNT1  (SYL_NEIG2) -  Leucine--tRNA ligase from Neisseria gonorrhoeae (strain NCCP11945)
Seq:
Struc:
 
Seq:
Struc:
876 a.a.
805 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.6.1.1.4  - leucine--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP + diphosphate
tRNA(Leu)
+ L-leucine
+ ATP
= L-leucyl-tRNA(Leu)
+ AMP
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

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