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PDBsum entry 4o2d

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protein ligands Protein-protein interface(s) links
Ligase PDB id
4o2d

 

 

 

 

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Contents
Protein chains
580 a.a.
515 a.a.
Ligands
ASP ×2
TRS ×4
Waters ×234
PDB id:
4o2d
Name: Ligase
Title: Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid
Structure: Aspartate--tRNA ligase. Chain: a, b. Synonym: aspartyl-tRNA synthetase, asprs. Engineered: yes
Source: Mycobacterium smegmatis. Organism_taxid: 246196. Strain: atcc 700084/ mc(2)155. Gene: asps, msmeg_3003, msmei_2928. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.60Å     R-factor:   0.198     R-free:   0.244
Authors: Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: L.Baugh et al. (2015). Increasing the structural coverage of tuberculosis drug targets. Tuberculosis (edinb), 95, 142-148. PubMed id: 25613812 DOI: 10.1016/j.tube.2014.12.003
Date:
17-Dec-13     Release date:   22-Jan-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0QWN3  (SYDND_MYCS2) -  Aspartate--tRNA(Asp/Asn) ligase from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Seq:
Struc:
 
Seq:
Struc:
598 a.a.
580 a.a.*
Protein chain
Pfam   ArchSchema ?
A0QWN3  (SYDND_MYCS2) -  Aspartate--tRNA(Asp/Asn) ligase from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Seq:
Struc:
 
Seq:
Struc:
598 a.a.
515 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.6.1.1.23  - aspartate--tRNA(Asn) ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + diphosphate
tRNA(Asx)
+
L-aspartate
Bound ligand (Het Group name = ASP)
corresponds exactly
+ ATP
= L-aspartyl-tRNA(Asx)
+ AMP
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.tube.2014.12.003 Tuberculosis (edinb) 95:142-148 (2015)
PubMed id: 25613812  
 
 
Increasing the structural coverage of tuberculosis drug targets.
L.Baugh, I.Phan, D.W.Begley, M.C.Clifton, B.Armour, D.M.Dranow, B.M.Taylor, M.M.Muruthi, J.Abendroth, J.W.Fairman, D.Fox, S.H.Dieterich, B.L.Staker, A.S.Gardberg, R.Choi, S.N.Hewitt, A.J.Napuli, J.Myers, L.K.Barrett, Y.Zhang, M.Ferrell, E.Mundt, K.Thompkins, N.Tran, S.Lyons-Abbott, A.Abramov, A.Sekar, D.Serbzhinskiy, D.Lorimer, G.W.Buchko, R.Stacy, L.J.Stewart, T.E.Edwards, W.C.Van Voorhis, P.J.Myler.
 
  ABSTRACT  
 
No abstract given.

 

 

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