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7A6Z

Structure of P226G 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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 301
ChainResidue
AGLN83
AASN86
AASP141
AASP240
ATYR272
AASP273
AGOL302
AHOH404
AHOH441

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 302
ChainResidue
AALA140
AASP141
AGLU275
APRO276
AGOL301
AHOH404
AHOH464
AHOH474
AHOH482
AHOH595

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 303
ChainResidue
APRO107
AGLN110
AGLN111
ATHR145
AALA146
ATHR149
AARG161
ALEU162
AASP163

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 304
ChainResidue
ATYR97
AVAL113
AVAL291
ALEU292
AALA293
AHOH406
AHOH412
AHOH593
AHOH603
AHOH615

site_idAC5
Number of Residues11
Detailsbinding site for residue GOL A 305
ChainResidue
AMET211
AALA212
AGLY217
AALA218
AARG222
AVAL231
AILE232
AASP233
AHOH413
AHOH419
AHOH478

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 306
ChainResidue
ATHR89
AHIS90
ALYS93
AASP273
AHOH411
AHOH473

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL A 307
ChainResidue
AALA30
AALA56
AILE57
AGLU59
ATYR60
AHOH409
AHOH461
AHOH467

site_idAC8
Number of Residues8
Detailsbinding site for residue GOL A 308
ChainResidue
AARG65
APRO174
AGLY175
AARG243
AHOH468
AHOH524
AHOH639
AHOH642

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 309
ChainResidue
AASP101
AASN136
AGLU165
AHOH484

site_idAD1
Number of Residues10
Detailsbinding site for residue PO4 A 310
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
AGLY236
ATHR237
AHOH401
AHOH462
AHOH630
AHOH645

site_idAD2
Number of Residues3
Detailsbinding site for residue PO4 A 311
ChainResidue
ALEU94
AGLY116
AGLN121

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 Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU166

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ASER130
ATHR235

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
ALYS73

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
AILE105

220113

PDB entries from 2024-05-22

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