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1M1Z

BETA-LACTAM SYNTHETASE APO ENZYME

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004066molecular_functionasparagine synthase (glutamine-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006529biological_processasparagine biosynthetic process
A0016874molecular_functionligase activity
A0033050biological_processclavulanic acid biosynthetic process
A0034027molecular_function(carboxyethyl)arginine beta-lactam-synthase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004066molecular_functionasparagine synthase (glutamine-hydrolyzing) activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006529biological_processasparagine biosynthetic process
B0016874molecular_functionligase activity
B0033050biological_processclavulanic acid biosynthetic process
B0034027molecular_function(carboxyethyl)arginine beta-lactam-synthase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP253
AASP351
BASP253
BASP351

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 303
ChainResidueDetails
ATYR348hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU382electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
ALYS443electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 303
ChainResidueDetails
BTYR348hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU382electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity

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PDB entries from 2025-06-18

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