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4ID4

Crystal structure of chimeric beta-lactamase cTEM-17m

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AARG93
ATHR141
ALEU174

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AGLY218
APRO219
ALEU220
AHOH431

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
AARG61
AHOH498

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AARG61
APRO62
AGLU63
AHOH506
AHOH752

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 305
ChainResidue
AARG244
AASN276
AHOH473
AHOH524

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 306
ChainResidue
AASP214
AHOH458
AHOH569
AHOH809
AHOH810

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS234

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 2
ChainResidueDetails
ASER70electrostatic stabiliser
ALYS73hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER130activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS234electrostatic stabiliser
AALA237electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-10-02

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