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3IXD

X-ray crystal structure of the extended-spectrum AmpC V298E mutant beta-lactamase at 2.64 Angstrom resolution

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 SO4 A 1
ChainResidue
ASER64
ATYR150
ALYS315
ATHR316
AGLY317
AALA318
AASN346
AHOH366
AHOH448

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 362
ChainResidue
ALYS164

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 363
ChainResidue
AVAL211
ASER212
ATHR319
AGLY320
AHOH365
AHOH436

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BSER64
BTYR150
BTHR316
BGLY317
BALA318
BHOH365
BHOH479

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 3
ChainResidue
BTRP93
BLEU161
BLYS164

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 362
ChainResidue
BVAL211
BSER212
BGLY320
BHOH367

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:6795623
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS315
BLYS315

219869

PDB entries from 2024-05-15

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