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3GQZ

AmpC beta-lactamase in complex with Fragment-based Inhibitor

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 Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 1
ChainResidue
AHIS13
ATHR42
AHOH592
AHOH745
BGLY116
BALA141

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 363
ChainResidue
BASP281
ATRP93
ALEU131
ALYS164

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GF7 A 362
ChainResidue
ALEU119
AARG148
ATYR150
AGLU272
ALYS290
AILE291
AALA292
ALEU293
AALA294
AHOH395
AHOH404
AHOH419
BASN9
BTYR40

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
AASN152
AALA318
BSER64
BTYR150
BASN152
BALA318
ATYR150

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PDB entries from 2024-06-12

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