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6NI1

Crystal Structure of the Beta Lactamase Class A penP from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 401
ChainResidue
AALA86
AALA189
AILE190
AASP193
ATHR197
AFMT402
AHOH522

site_idAC2
Number of Residues6
Detailsbinding site for residue FMT A 402
ChainResidue
APRO191
AASN281
AEDO401
AHOH524
AARG63
AALA189

site_idAC3
Number of Residues6
Detailsbinding site for residue FMT A 403
ChainResidue
ASER46
ATHR49
AASN50
APHE53
AALA78
AHOH581

site_idAC4
Number of Residues2
Detailsbinding site for residue FMT B 401
ChainResidue
BASP61
BARG282

site_idAC5
Number of Residues1
Detailsbinding site for residue FMT B 402
ChainResidue
BLYS137

site_idAC6
Number of Residues2
Detailsbinding site for residue FMT B 403
ChainResidue
AASP286
BARG229

site_idAC7
Number of Residues3
Detailsbinding site for residue FMT B 404
ChainResidue
BASP185
BTHR218
BARG221

site_idAC8
Number of Residues4
Detailsbinding site for residue FMT B 405
ChainResidue
BALA189
BILE190
BASP193
BHOH514

site_idAC9
Number of Residues1
Detailsbinding site for residue FMT B 406
ChainResidue
BHOH582

site_idAD1
Number of Residues3
Detailsbinding site for residue FMT B 407
ChainResidue
AVAL120
AGLU127
BASN288

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaYASTyKvlaAAAVL
ChainResidueDetails
APHE85-LEU100

227344

PDB entries from 2024-11-13

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