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5F1G

Crystal structure of AmpC BER adenylylated in the cytoplasm

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue AMP A 401
ChainResidue
ASER61
ATHR318
ASO4402
AHOH502
AHOH505
AHOH580
AHOH615
AHOH631
AHOH636
AHOH638
AGLN117
AVAL118
AASP120
ATYR147
AASN149
ATYR218
AGLY316
AALA317

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 402
ChainResidue
AVAL208
ASER209
AGLY319
AAMP401
AHOH521
AHOH580

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 403
ChainResidue
AARG201
AGLU202
AHOH513
AHOH667

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO A 404
ChainResidue
ATRP90
ALYS161

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

224201

PDB entries from 2024-08-28

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