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3NY4

Crystal Structure of BlaC-K73A bound with Cefamandole

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AHOH8
AHOH12
AARG79
AARG187
AGLU193
AASP255
ATYR286
ASMX308

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SMX A 308
ChainResidue
AHOH40
ASER84
AILE117
ASER142
AASN186
ATHR232
AARG236
ALYS250
ATHR251
AGLY252
ATHR253
AGLY254
AASP255
ASMX309
ASMX311
AHOH318
AHOH508
APO41

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SMX A 309
ChainResidue
AILE117
AARG177
AASP192
AGLU193
AARG194
AARG236
AGLU289
AGLU292
ASMX308
ASMX311

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SMX A 310
ChainResidue
APRO157
AALA162
AVAL210
ALEU211
AARG220
ATHR224
ALYS246
ATRP266
AGLY270
ASMX312
AHOH409

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SMX A 311
ChainResidue
AARG194
ASMX308
ASMX309
ASMX312
AHOH494
AHOH495

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SMX A 312
ChainResidue
AALA162
ATHR165
AARG169
ATHR224
AASP225
AALA228
ALYS246
AILE248
AARG281
AASP287
AALA288
AGLU289
AARG291
ASMX310
ASMX311
AHOH509

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
ASER84

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU182

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER142
ATHR251

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AALA87

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
AILE117

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PDB entries from 2024-05-15

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