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3GTC

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 Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AARG133
AHIS186
AHOH618
AHOH683
AHOH686
AHOH687
AHOH692
BLYS290
BHOH428

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GTC A 362
ChainResidue
AHOH2
AHIS210
AVAL211
ASER212
ATYR221
ATHR319
AGLY320
AGTC364
AHOH627
AHOH716

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 363
ChainResidue
ASER64
ATYR150
ATHR316
AGLY317
AALA318
AHOH487

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GTC A 364
ChainResidue
ASER64
ALEU119
AALA318
ATHR319
AGTC362
AHOH487

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GTC B 1
ChainResidue
BSER64
BGLN120
BLEU293
BALA318
BTHR319
BHOH629
BHOH637
BHOH664

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GTC B 362
ChainResidue
BTYR92
BTRP93
BGLU95
BSER128
BLEU131
BLEU157
BLEU161
BLYS164

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GTC B 363
ChainResidue
ATYR92
ATRP93
AGLU95
ASER128
ALEU131
ALEU161
ALYS164
AHOH638
BASN279
BASP281

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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