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8OE1

Structure of P167S BlaC from Mycobacterium tuberculosis at pH 5

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
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0008800molecular_functionbeta-lactamase activity
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
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 Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER70
CSER70

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU166
CGLU166

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER130
ATHR235
CSER130
CTHR235

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
ALYS73
CLYS73

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821
ChainResidueDetails
AILE105
CILE105

219869

PDB entries from 2024-05-15

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