Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
FOA 2-furoic acid
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 4RM3   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Crystal structure of a benzoate coenzyme A ligase with 2-Furoic acid
Release Data : 2015-09-30
Compound :
mol_id molecule chains
1 Benzoate-coenzyme A ligase A,B
Source :
mol_id organism_scientific expression_system
1 Rhodopseudomonas palustris  (taxid:1076) Escherichia coli  (taxid:562)
gene: badA
expression_system_vector_type: plasmid
expression_system_plasmid: pET28a
Authors : Strom, S., Nosrati, M., Thornburg, C., Walker, K.D., Geiger, J.H.
Keywords : Substrate Specificity, Kinetics, LYASE
Exp. method : X-RAY DIFFRACTION ( 1.76 Å )
Citation :

Kinetically and Crystallographically Guided Mutations of a Benzoate CoA Ligase (BadA) Elucidate Mechanism and Expand Substrate Permissivity.

Thornburg, C.K.,Wortas-Strom, S.,Nosrati, M.  et al.
(2015)  Biochemistry  54 : 6230 - 6242

PubMed: 26378464
DOI: 10.1021/acs.biochem.5b00899

Chain : A, B
UniProt : Q93TK0 (Q93TK0_RHOPL)
Reaction : -