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6B68

Beta-Lactamase, 100ms timepoint, mixed, shards crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0033250molecular_functionpenicillinase activity
A0033251molecular_functioncephalosporinase activity
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0008800molecular_functionbeta-lactamase activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0033250molecular_functionpenicillinase activity
B0033251molecular_functioncephalosporinase activity
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0008800molecular_functionbeta-lactamase activity
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030655biological_processbeta-lactam antibiotic catabolic process
C0033250molecular_functionpenicillinase activity
C0033251molecular_functioncephalosporinase activity
C0042597cellular_componentperiplasmic space
C0046677biological_processresponse to antibiotic
D0005576cellular_componentextracellular region
D0005886cellular_componentplasma membrane
D0008800molecular_functionbeta-lactamase activity
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0030655biological_processbeta-lactam antibiotic catabolic process
D0033250molecular_functionpenicillinase activity
D0033251molecular_functioncephalosporinase activity
D0042597cellular_componentperiplasmic space
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue PO4 A 301
ChainResidue
ASER70
ASER128
ALYS236
ATHR237
AGLY238
ATHR239
BGLN109

site_idAC2
Number of Residues11
Detailsbinding site for residue 9F2 A 302
ChainResidue
AASN216
ATHR217
AHOH470
BPRO105
BTYR127
BTHR217
BTHR218
B9F2301
BFZS302
AARG126
ATYR127

site_idAC3
Number of Residues14
Detailsbinding site for residue 9F2 B 301
ChainResidue
AGLN109
A9F2302
BSER70
BSER128
BPRO169
BASN172
BTHR218
BLYS236
BTHR237
BGLY238
BTHR239
BGLY240
BFZS302
BHOH451

site_idAC4
Number of Residues15
Detailsbinding site for residue FZS B 302
ChainResidue
AGLN109
A9F2302
BCYS69
BSER70
BSER128
BPRO169
BASN172
BLYS236
BTHR237
BGLY238
BTHR239
BGLY240
B9F2301
BHOH413
BHOH451

site_idAC5
Number of Residues6
Detailsbinding site for residue PO4 C 301
ChainResidue
CSER70
CSER128
CLYS236
CTHR237
CTHR239
DGLN109

site_idAC6
Number of Residues8
Detailsbinding site for residue 9F2 C 302
ChainResidue
CARG126
CTYR127
CTHR217
CHOH437
DTHR217
DTHR218
DASP241
D9F2400

site_idAC7
Number of Residues16
Detailsbinding site for residue 9F2 D 400
ChainResidue
C9F2302
DSER70
DSER128
DPRO169
DASN172
DARG173
DTHR218
DLYS236
DTHR237
DGLY238
DTHR239
DGLY240
DASP241
DGLU278
DHOH504
DHOH542

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER70
BSER70
CSER70
DSER70

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU168
BGLU168
CGLU168
DGLU168

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
CSER128
CTHR237
DSER128
DTHR237
ASER128
ATHR237
BSER128
BTHR237

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
ALYS73
BLYS73
CLYS73
DLYS73

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821
ChainResidueDetails
AILE103
BILE103
CILE103
DILE103

218500

PDB entries from 2024-04-17

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