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4QB8

Crystal Structure of beta-lactamase from M.tuberculosis forming Michaelis Menten with Tebipenem

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 PO4 A 401
ChainResidue
AARG79
AARG187
AGLU193
AASP255
ATYR286
AHOH643
AHOH702
AHOH703
AHOH798

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AARG53
AGLN133
AHOH517
AHOH554
AHOH591
AHOH717
AHOH751
AHOH812

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 403
ChainResidue
AARG140
ATYR141
AHOH509
AHOH517
AHOH554

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 404
ChainResidue
AARG75
AGLU78
AARG115
AGLU184

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1TE A 405
ChainResidue
ASER84
AILE117
ASER142
AGLU182
ATHR251
AGLY252
ATHR253
AHOH693
AHOH699
AHOH700
AHOH701
AHOH711
AHOH796

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
ASER84

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AGLU182

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19251630, ECO:0000269|PubMed:20353175, ECO:0000269|PubMed:20961112
ChainResidueDetails
ATHR251
ASER142

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Ser => ECO:0000303|PubMed:20353175, ECO:0000303|PubMed:20961112
ChainResidueDetails
AALA87

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
AILE117

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PDB entries from 2024-06-12

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