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7CIN

Crystal structure of the extended-spectrum class C beta-lactamase AmpC BER with the ordered R2 loop

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
B0000166molecular_functionnucleotide binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 401
ChainResidue
AARG201
AVAL208
ASER209
AGLY319
AHOH664

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 402
ChainResidue
AGLY316
AHOH505
AHOH517
AHOH709
AHOH711
ASER61
ATYR147
ALYS314
ATHR315

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 B 401
ChainResidue
BSER61
BTYR147
BLYS314
BTHR315
BGLY316
BALA317
BHOH506

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

219869

PDB entries from 2024-05-15

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