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6B6A

Beta-Lactamase, 2secs 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
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
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
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
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 Residues14
Detailsbinding site for residue 9F2 A 302
ChainResidue
AASN216
ATHR217
AHOH404
AHOH414
BILE103
BPRO105
BTYR127
BTHR217
BTHR218
BASP241
B9F2301
BFZS302
AARG126
ATYR127

site_idAC3
Number of Residues15
Detailsbinding site for residue 9F2 B 301
ChainResidue
AGLN109
A9F2302
BSER70
BSER128
BPRO169
BASN172
BTHR218
BLYS236
BTHR237
BGLY238
BTHR239
BGLY240
BASP241
BFZS302
BHOH455

site_idAC4
Number of Residues16
Detailsbinding site for residue FZS B 302
ChainResidue
AGLN109
A9F2302
BCYS69
BSER70
BSER128
BPRO169
BASN172
BLYS236
BTHR237
BGLY238
BTHR239
BGLY240
BASP241
B9F2301
BHOH406
BHOH455

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

site_idAC6
Number of Residues12
Detailsbinding site for residue 9F2 C 302
ChainResidue
CARG126
CTYR127
CASN216
CTHR217
CHOH456
DILE103
DPRO105
DTHR217
DTHR218
DASP241
D9F2301
DFZS302

site_idAC7
Number of Residues19
Detailsbinding site for residue 9F2 D 301
ChainResidue
CGLN109
C9F2302
DSER70
DILE103
DSER128
DPRO169
DASN172
DTHR218
DLYS236
DTHR237
DGLY238
DTHR239
DGLY240
DASP241
DGLU278
DFZS302
DHOH404
DHOH421
DHOH451

site_idAC8
Number of Residues19
Detailsbinding site for residue FZS D 302
ChainResidue
DTHR237
DGLY238
DTHR239
DGLY240
DASP241
D9F2301
DHOH404
DHOH414
DHOH421
CGLN109
C9F2302
DCYS69
DSER70
DLYS73
DILE103
DSER128
DPRO169
DASN172
DLYS236

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
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Increases nucleophilicity of active site Ser","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site","evidences":[{"source":"PubMed","id":"24023821","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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