Structure of PDB 3wo1 Chain A

Receptor sequence
>3wo1A (length=466) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
SKTVLVIADLGGCPPHMFYKSAAEKYNLVSFIPRPFAITASHAALIEKYS
VAVIKDKDYFKSLADFEHPDSIYWAHEDHNKPEEEVVEQIVKVAEMFGAD
AITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKS
IKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEDEFN
RVNDYLKSINVPKAVTFEAPFIAEEFLQGEYGDWYQTEGYSDYISIEGIM
ADGEYFPIAIHDKTPQIGFTETSHITPSILDEEAKKKIVEAAKKANEGLG
LQNCATHTEIKLMKNREPGLIESAARFAGANMIPNIKKVFGLDMAQLLLD
VLCFGKDADLPDGLLDQEPYYVADCHLYPQHFKQNGQIPETAEDLVIEAI
DIPDGLLKGDTEIVSFSAAAPGTSVDLTLFEAFNSIAAFELKGSNSQDVA
ESIRQIQQHAKLTAKY
3D structure
PDB3wo1 Single Mutation Alters the Substrate Specificity of l-Amino Acid Ligase
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.49: L-alanine--L-anticapsin ligase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ADP A K178 S184 S185 F228 L229 Q268 E311 E324 K176 S182 S183 F226 L227 Q266 E309 E322
BS02 MG A E311 E324 E309 E322
BS03 ALA A E273 H309 R328 G331 E271 H307 R326 G329
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0034026 L-amino-acid alpha-ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3wo1, PDBe:3wo1, PDBj:3wo1
PDBsum3wo1
PubMed24702628
UniProtP39641|BACD_BACSU Alanine--anticapsin ligase (Gene Name=bacD)

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