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5OYO

Crystal structure of 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
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
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ACT A 401
ChainResidue
ALYS232
AVAL233
APGE406
BTHR96

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 402
ChainResidue
AARG44
AGLU64
AARG65

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 403
ChainResidue
AALA268
AGLY269
AALA43
AARG44

site_idAC4
Number of Residues6
Detailsbinding site for residue ACT A 404
ChainResidue
ASER70
ASER128
ALYS236
ATHR237
AGLY238
ATHR239

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
AALA31
AALA57
AILE58
AGLU59

site_idAC6
Number of Residues8
Detailsbinding site for residue PGE A 406
ChainResidue
AALA214
AGLY219
AALA220
AARG224
AVAL233
AASP235
AACT401
AHOH535

site_idAC7
Number of Residues4
Detailsbinding site for residue ACT B 401
ChainResidue
BASP99
BARG101
BASN134
BGLU167

site_idAC8
Number of Residues2
Detailsbinding site for residue ACT B 402
ChainResidue
APRO203
BGLY177

site_idAC9
Number of Residues5
Detailsbinding site for residue ACT B 403
ChainResidue
BSER128
BLYS236
BTHR237
BGLY238
BTHR239

site_idAD1
Number of Residues7
Detailsbinding site for residue PGE B 404
ChainResidue
BLEU157
BGLY158
BASP159
BALA187
BLEU190
BVAL191
BGLN194

site_idAD2
Number of Residues3
Detailsbinding site for residue PGE B 405
ChainResidue
BTHR210
BLYS232
BTRP252

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
BSER70

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

226262

PDB entries from 2024-10-16

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