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5GGW

Crystal structure of Class C beta-lactamase

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
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 Residues4
Detailsbinding site for residue SO4 A 401
ChainResidue
AVAL208
ASER209
AGLY317
AHOH551

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 402
ChainResidue
AALA315
AHOH502
ASER61
ATYR147
ALYS312
ATHR313
AGLY314

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
BVAL208
BSER209
BTHR316
BGLY317
BHOH516

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 B 402
ChainResidue
BSER61
BTYR147
BLYS312
BTHR313
BGLY314
BALA315
BHOH506

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

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PDB entries from 2024-11-06

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