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6H27

Structure of S70C BlaC from Mycobacterium tuberculosis

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
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0033250molecular_functionpenicillinase activity
B0033251molecular_functioncephalosporinase activity
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 401
ChainResidue
ACYS70
ASER128
ATHR237
AGLY238
ATHR239
AHOH504

site_idAC2
Number of Residues8
Detailsbinding site for residue PG0 A 402
ChainResidue
ALYS205
AARG224
AALA229
AHOH525
AHOH546
AGLN83
AASN84
APRO85

site_idAC3
Number of Residues10
Detailsbinding site for residue PG0 B 401
ChainResidue
BARG33
BGLU36
BLEU37
BGLY152
BARG155
BSER156
BGLU283
BTHR286
BCYS287
BHOH579

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
ACYS70
BCYS70

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU168
BGLU168

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER128
ATHR237
BSER128
BTHR237

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
ALYS73
BLYS73

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
AILE103
BILE103

222926

PDB entries from 2024-07-24

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