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6H2I

Structure of BlaC from Mycobacterium tuberculosis bound to the trans-enamine adduct of tazobactam.

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue TBE A 501
ChainResidue
ASER70
AASP241
AACT502
ASER102
AILE103
ASER128
AGLU168
AASN172
AARG173
AGLY238
ATHR239

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 502
ChainResidue
ASER70
ASER128
ALYS236
ATHR237
AGLY238
ATHR239
ATBE501

site_idAC3
Number of Residues7
Detailsbinding site for residue ACT B 502
ChainResidue
BSER70
BSER128
BLYS236
BTHR237
BGLY238
BTHR239
BTBE501

site_idAC4
Number of Residues16
Detailsbinding site for Di-peptide TBE B 501 and SER B 70
ChainResidue
BPHE68
BCYS69
BTHR71
BPHE72
BLYS73
BILE103
BSER128
BGLU168
BPRO169
BASN172
BARG173
BLYS236
BTHR237
BTHR239
BASP241
BACT502

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

219869

PDB entries from 2024-05-15

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