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Crystal structure of L2 complexed with relebactam (16 hour soak)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue DSN A 301
ChainResidue
ACYS69
ASER70
ASER130
AGLY236
ASER237
AHOH404
AHOH411
AHOH501

site_idAC2
Number of Residues19
Detailsbinding site for Di-peptide MK7 B 301 and SER B 70
ChainResidue
BMET68
BCYS69
BTHR71
BPHE72
BLYS73
BHIS105
BSER130
BASN132
BASN170
BTHR216
BLYS234
BTHR235
BGLY236
BSER237
BHOH405
BHOH417
BHOH430
BHOH497
AGLY175

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMCSTfKsmlAATVL
ChainResidueDetails
APHE66-LEU81

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PDB entries from 2024-09-04

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