Structure of PDB 3wo0 Chain A

Receptor sequence
>3wo0A (length=465) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
KTVLVIADLGGCPPHMFYKSAAEKYNLVSFIPRPFAITASHAALIEKYSV
AVIKDKDYFKSLADFEHPDSIYWAHEDHNKPEEEVVEQIVKVAEMFGADA
ITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSI
KNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEDEFNR
VNDYLKSINVPKAVTFEAPFIAEEFLQGEYGDWYQTEGYSDYISIEGIMA
DGEYFPIAIHDKTPQIGFTETSHITPSILDEEAKKKIVEAAKKANEGLGL
QNCATHTEIKLMKNREPGLIESAARFAGWNMIPNIKKVFGLDMAQLLLDV
LCFGKDADLPDGLLDQEPYYVADCHLYPQHFKQNGQIPETAEDLVIEAID
IPDGLLKGDTEIVSFSAAAPGTSVDLTLFEAFNSIAAFELKGSNSQDVAE
SIRQIQQHAKLTAKY
3D structure
PDB3wo0 Single Mutation Alters the Substrate Specificity of l-Amino Acid Ligase
ChainA
Resolution2.0 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 K138 I176 K178 A183 S184 S185 E226 F228 L229 Q268 F271 I323 E324 K135 I173 K175 A180 S181 S182 E223 F225 L226 Q265 F268 I320 E321
BS02 MG A E311 E324 E308 E321
BS03 ALA A E273 H309 E311 R328 G331 E270 H306 E308 R325 G328
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:3wo0, PDBe:3wo0, PDBj:3wo0
PDBsum3wo0
PubMed24702628
UniProtP39641|BACD_BACSU Alanine--anticapsin ligase (Gene Name=bacD)

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