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2RCX

AmpC Beta-lactamase in complex with (1R)-1-(2-Thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)-phenyl) methylboronic 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 Residues12
DetailsBINDING SITE FOR RESIDUE SM4 A 964
ChainResidue
APO41
AGLY320
AASN343
AHOH1125
ASER64
ALEU119
ATYR150
AASN152
ATYR221
AASN289
AGLY317
AALA318

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
ASER64
ATYR150
ALYS315
ATHR316
AGLY317
AALA318
ASM4964
AHOH1187

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 362
ChainResidue
AHIS186
AHOH1025
AHOH1030
AHOH1044
AHOH1114
AHOH1227
BLYS290

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SM4 B 964
ChainResidue
BSER64
BLEU119
BGLN120
BTYR150
BASN152
BTYR221
BASN289
BGLY317
BALA318
BTHR319
BGLY320
BASN343
BHOH1143

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 2024-06-12

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