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1FCM

CRYSTAL STRUCTURE OF THE E.COLI AMPC BETA-LACTAMASE MUTANT Q120L/Y150E COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, CLOXACILLIN

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 Residues13
DetailsBINDING SITE FOR RESIDUE CXU A 961
ChainResidue
ASER61
AASN340
AASN343
AHOH964
BALA1
ALEU116
ALEU117
AGLU147
AASN149
ATYR218
ATHR313
AGLY314
AALA315

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CXU B 961
ChainResidue
BSER61
BLEU117
BGLU147
BASN149
BTYR218
BASN286
BLYS312
BTHR313
BGLY314
BALA315
BTHR316
BASN340
BASN343
BHOH977
BHOH1007
BHOH1028
BHOH1033

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE57-LYS64

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
ASER61
BSER61

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER61
AGLU147
AASN149
AALA315
BSER61
BGLU147
BASN149
BALA315

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
ASER61
ALYS64
AGLU269
AGLU147
ALYS312

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
BSER61
BLYS64
BGLU269
BGLU147
BLYS312

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PDB entries from 2024-07-17

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