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6B6E

Beta-Lactamase, mixed with Ceftriaxone, needles crystal form, 500ms

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue FZS A 301
ChainResidue
ACYS69
ATHR239
AGLY240
A9F2302
AHOH437
AHOH444
AHOH450
ASER70
AILE103
ASER128
APRO169
AASN172
ALYS236
ATHR237
AGLY238

site_idAC2
Number of Residues20
Detailsbinding site for residue 9F2 A 302
ChainResidue
ASER70
AILE103
ASER128
APRO169
AASN172
AARG173
AARG222
ALYS236
ATHR237
AGLY238
ATHR239
AGLY240
AASP241
AFZS301
AHOH437
AHOH444
AHOH461
AHOH499
AHOH526
AHOH533

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 Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU168

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER128
ATHR237

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
ALYS73

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821
ChainResidueDetails
AILE103

218196

数据于2024-04-10公开中

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