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3GRJ

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
ASER64
ATYR150
AASN289
ALYS315
ATHR316
AGLY317
AALA318
AHOH471

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 362
ChainResidue
ALEU131
ALEU161
ALYS164
ATRP93

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PO4 A 363
ChainResidue
AARG80

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE G14 A 1
ChainResidue
ASER129
AARG133
AHIS186
AHOH489
BLYS290

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 364
ChainResidue
APRO140
AALA141
AALA143
AHOH486
AHOH487

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE G14 A 365
ChainResidue
ASER166
AGLY167
ALEU168
AHOH488
BASN358
BALA359
BGLN361

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 1
ChainResidue
BSER64
BTYR150
BTHR316
BGLY317
BALA318
BG14363
BHOH412

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 3
ChainResidue
AARG14
BARG80
BHOH404

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 362
ChainResidue
BSER127
BSER128

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE G14 B 363
ChainResidue
BPO41
BSER64
BGLN120
BTYR150
BASN152
BDMS368

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS B 364
ChainResidue
AASP288
AASN289
ALEU293
BTYR40
BHOH482

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 365
ChainResidue
BPRO140
BTRP142
BALA143
BHOH466
BHOH468

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG B 366
ChainResidue
BARG148
BTYR150
BGLU272
BILE283
BGLY286
BSER287
BALA292
BHIS314
BHOH396
BHOH475
BHOH481

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS B 367
ChainResidue
BGLU205

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS B 368
ChainResidue
BGLN120
BG14363

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
AASN152
AALA318
BSER64
BTYR150
BASN152
BALA318
ASER64
ATYR150

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PDB entries from 2024-06-12

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