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2V1Z

Structure of a TEM-1 beta-lactamase insertant allosterically regulated by kanamycin and anions.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1271
ChainResidue
AGLU90
AHIS133
AHIS138
AHOH2352

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
ChainResidueDetails
APHE46-LEU61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER50

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU148

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS214

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ALYS53
ASER110
ASER50
AGLU146

site_idMCSA1
Number of Residues6
DetailsM-CSA 2
ChainResidueDetails
ASER50electrostatic stabiliser
ALYS53hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER110activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU146activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS214electrostatic stabiliser
AALA217electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-31

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