Brand  (β version)

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Ligands
Code Name Style Show Link
07K 8-methylquinolin-4-amine
CL Chloride ion
NA Sodium ion
Non-standard Residues
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Glycosylation
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Code : 3U0E   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of beta-ketoacyl synthase from Brucella melitensis in complex with fragment 9320
Release Data : 2011-10-26
Compound :
mol_id molecule chains
1 Beta-ketoacyl synthase A
ec: 2.3.1.41
Source :
mol_id organism_scientific expression_system
1 Brucella melitensis biovar Abortus  (taxid:359391) Escherichia coli  (taxid:469008)
strain: 2308
gene: fabB, BAB1_2173
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: AVA0421
Authors : Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Keywords : BETA-KETOACYL SYNTHASE, BRUCELLA MELITENSIS, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, Fragments of Life, 8-methylquinolin-4-amine, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.60 Å )
Citation :

Structural characterization of beta-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.

Patterson, E.I.,Nanson, J.D.,Abendroth, J.  et al.
(2020)  Proteins  88 : 47 - 56

PubMed: 31237717
DOI: 10.1002/prot.25765

Chain : A
UniProt : Q2YQQ9 (Q2YQQ9_BRUA2)
Reaction: EC: Evidence:
Physiological Direction:
(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)- dodecenoyl-[ACP] + CO2 + holo-[ACP] - ARBA:ARBA00035917
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a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP] 2.3.1.41 ARBA:ARBA00023389
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