PDBsum entry 3qmn

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
Protein chains
(+ 18 more) 126 a.a. *
COA ×24
MPD ×16
ACT ×8
MRD ×6
_CA ×46
_CL ×9
Waters ×2555
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of 4'-phosphopantetheinyl transferase acps vibrio cholerae o1 biovar eltor
Structure: Holo-[acyl-carrier-protein] synthase. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r v, w, x. Synonym: holo-acp synthase, 4'-phosphopantetheinyl transfer engineered: yes
Source: Vibrio cholerae o1 biovar el tor. Organism_taxid: 243277. Strain: n16961. Gene: acps, vc_2457. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.85Å     R-factor:   0.158     R-free:   0.191
Authors: Y.Kim,A.S.Halavaty,M.Zhou,K.Kwon,W.F.Anderson,A.Joachimiak,C Structural Genomics Of Infectious Diseases (Csgid)
Key ref: A.S.Halavaty et al. (2012). Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria. Acta Crystallogr D Biol Crystallogr, 68, 1359-1370. PubMed id: 22993090
04-Feb-11     Release date:   02-Mar-11    
Supersedes: 3ota
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9KPB6  (ACPS_VIBCH) -  Holo-[acyl-carrier-protein] synthase
126 a.a.
126 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Holo-[acyl-carrier-protein] synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]
+ apo-[acyl-carrier-protein]
adenosine 3',5'-bisphosphate
Bound ligand (Het Group name = COA)
matches with 56.25% similarity
+ holo-[acyl-carrier-protein]
      Cofactor: Magnesium
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     lipid metabolic process   5 terms 
  Biochemical function     transferase activity     4 terms  


    Added reference    
Acta Crystallogr D Biol Crystallogr 68:1359-1370 (2012)
PubMed id: 22993090  
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
A.S.Halavaty, Y.Kim, G.Minasov, L.Shuvalova, I.Dubrovska, J.Winsor, M.Zhou, O.Onopriyenko, T.Skarina, L.Papazisi, K.Kwon, S.N.Peterson, A.Joachimiak, A.Savchenko, W.F.Anderson.
Some bacterial type II fatty-acid synthesis (FAS II) enzymes have been shown to be important candidates for drug discovery. The scientific and medical quest for new FAS II protein targets continues to stimulate research in this field. One of the possible additional candidates is the acyl-carrier-protein synthase (AcpS) enzyme. Its holo form post-translationally modifies the apo form of an acyl carrier protein (ACP), which assures the constant delivery of thioester intermediates to the discrete enzymes of FAS II. At the Center for Structural Genomics of Infectious Diseases (CSGID), AcpSs from Staphylococcus aureus (AcpS(SA)), Vibrio cholerae (AcpS(VC)) and Bacillus anthracis (AcpS(BA)) have been structurally characterized in their apo, holo and product-bound forms, respectively. The structure of AcpS(BA) is emphasized because of the two 3',5'-adenosine diphosphate (3',5'-ADP) product molecules that are found in each of the three coenzyme A (CoA) binding sites of the trimeric protein. One 3',5'-ADP is bound as the 3',5'-ADP part of CoA in the known structures of the CoA-AcpS and 3',5'-ADP-AcpS binary complexes. The position of the second 3',5'-ADP has never been described before. It is in close proximity to the first 3',5'-ADP and the ACP-binding site. The coordination of two ADPs in AcpS(BA) may possibly be exploited for the design of AcpS inhibitors that can block binding of both CoA and ACP.