Structure of PDB 1mbz Chain A

Receptor sequence
>1mbzA (length=496) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence]
APVLPAAFGFLASARTGGPVFATRGSHTDIDTPQGERSLAATLVHAPSVA
PDRAVARSLTGAPTTAVLAGEIYNRDELLSVLPAGPAPEGDAELVLRLLE
RYDLHAFRLVNGRFATVVRTGDRVLLATDHAGSVPLYTCVAPGEVRASTE
AKALAAHGFPLADARRVAGLTGVYQVPAGAVMDIDLGSGTAVTHRTWTPG
LSRRILPEGEAVAAVRAALEKAVAQRVTPGDTPLVVLSGGIDSSGVAACA
HRAAGELDTVSMGTDTSNEFREARAVVDHLRTRHREITIPTTELLAQLPY
AVWASESVDPDIIEYLLPLTALYRALDGPERRILTGYGADIPLGGMHRED
RLPALDTVLAHDMATFDGLNEMSPVLSTLAGHWTTHPYWDREVLDLLVSL
EAGLKRRHGRDKWVLRAAMADALPAETVNRPKLGVHEGSGTTSSFSRLLL
DHGVAEDRVHEAKRQVVRELFDLTVGGGRHPSEVDTDDVVRSVADR
3D structure
PDB1mbz The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots
ChainA
Resolution2.47 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 D311 Y337 E371 K432
Enzyme Commision number 6.3.3.4: (carboxyethyl)arginine beta-lactam-synthase.
Interaction with ligand
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:1mbz, PDBe:1mbz, PDBj:1mbz
PDBsum1mbz
PubMed12409610
UniProtP0DJQ7|BLS_STRCL Carboxyethyl-arginine beta-lactam-synthase (Gene Name=bls)

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