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7A5T

Crystal structure of A55E mutant 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 301
ChainResidue
AASP240
ATYR272
AASP273
AHOH406

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 302
ChainResidue
APRO276
AGLU278
AHOH414
AHOH494

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 303
ChainResidue
AGLN110
AGLN111
AHOH558
APRO107

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 304
ChainResidue
ATHR89
AHIS90
AASP92
AHOH409
AHOH415

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 305
ChainResidue
AALA140
AASP141
AHOH460

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 306
ChainResidue
AALA223
APRO226
ATHR286
AHOH435

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 307
ChainResidue
ASER70
ALYS73
AILE105
ASER130
AGLY132
AGLU166
AASN170
AGOL309
APO4310

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 308
ChainResidue
AGLY156
AASP157
ATHR158
AHIS184
AHOH421
AHOH505

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL A 309
ChainResidue
AASN170
AARG171
ATHR237
AASP240
AGOL307

site_idAD1
Number of Residues8
Detailsbinding site for residue PO4 A 310
ChainResidue
ASER70
ASER130
ALYS234
ATHR235
AGLY236
ATHR237
AGOL307
AHOH471

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

224201

PDB entries from 2024-08-28

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