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3WS5

N288Q-N321Q mutant BETA-LACTAMASE DERIVED FROM CHROMOHALOBACTER SP.560 (Condition-2B)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030288cellular_componentouter membrane-bounded periplasmic space
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SR A 401
ChainResidue
AASP219
AASP220
AHOH539

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AVAL122

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP291
BGLU295
BGLU352

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 402
ChainResidue
BVAL122
BASN153

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 401
ChainResidue
CPHE121
CVAL122
CASN153

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSLSK
ChainResidueDetails
APHE61-LYS68

223166

PDB entries from 2024-07-31

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