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4LV0

AmpC beta-lactamase in complex with m-aminophenyl boronic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE APB A 401
ChainResidue
ASER64
ATYR150
AASN152
ATYR221
AALA318
AHOH651
AHOH655
AHOH740
AHOH926

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AARG133
AHIS186
AHOH587
AHOH656
AHOH804
AHOH870
AHOH880
BLYS290

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE APB B 401
ChainResidue
BSER64
BTYR150
BASN152
BTYR221
BALA318
BHOH613
BHOH652

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
ATYR150
AASN152
AALA318
BSER64
BTYR150
BASN152
BALA318

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PDB entries from 2024-07-24

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