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1N4O

Crystal structure of the Class A beta-lactamase L2 from Stenotrophomonas maltophilia

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 Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 1001
ChainResidue
BSER70
BHOH1160
BHOH1168
BSER130
BLYS234
BTHR235
BGLY236
BSER237
BHOH1007
BHOH1009
BHOH1011

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
AGLY236
ASER237
AHOH1005
AHOH1007
AHOH1009

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1003
ChainResidue
BARG178
BHOH1032

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AARG178
AHOH1030

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 2024-04-10

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