Structure of PDB 1jgt Chain A

Receptor sequence
>1jgtA (length=490) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
PVLPAAFGFLASARTGGGPVFATRGSHTDIDTPQGERSLAATLVHAPSVA
PDRAVARSLTGAPTTAVLAGEIYNRDELLSVLPAGPAPEGDAELVLRLLE
RYDLHAFRLVNGRFATVVRTGDRVLLATDHAGSVPLYTCVAPGEVRASTE
AKALAAHPKGFPLADARRVAGLTGVYQVPAGAVMDIDLGSGTAVTHRTWT
PGLSRRILPEGEAVAAVRAALEKAVAQRVTPGDTPLVVLSGGIDSSGVAA
CAHRAAGELDTVSMGTDTSNEFREARAVVDHLRTRHREITIPTTELLAQL
PYAVWASESVDPDIIEYLLPLTALYRALDGPERRILTGYGADIPLGGMHR
EDRLPALDTVLAHDMATFDGLNEMSPVLSTLAGHWTTHPYWDREVLDLLV
SLEAGLKRRHGRDKWVLRAAMADALPAETVNRPKLSSFSRLLLDHGVAED
RVHEAKRQVVRELFDLTVGGGRHPSEVDTDDVVRSVADRT
3D structure
PDB1jgt Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A76 G77 D322 Y348 E382 K443
Catalytic site (residue number reindexed from 1) A69 G70 D313 Y339 E373 K434
Enzyme Commision number 6.3.3.4: (carboxyethyl)arginine beta-lactam-synthase.
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 MG A D253 D351 D244 D342
BS02 APC A V247 L248 S249 G251 I252 D253 S254 S272 M273 L330 G347 Y348 D351 K423 K443 V238 L239 S240 G242 I243 D244 S245 S263 M264 L321 G338 Y339 D342 K414 K434
BS03 CMA A Y326 Y348 G349 D351 I352 D373 E382 Y317 Y339 G340 D342 I343 D364 E373
Gene Ontology
Molecular Function
GO:0004066 asparagine synthase (glutamine-hydrolyzing) activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0034027 (carboxyethyl)arginine beta-lactam-synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0006529 asparagine biosynthetic process
GO:0033050 clavulanic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1jgt, PDBe:1jgt, PDBj:1jgt
PDBsum1jgt
PubMed11473258
UniProtP0DJQ7|BLS_STRCL Carboxyethyl-arginine beta-lactam-synthase (Gene Name=bls)

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