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7TI1

Structure of AmpC bound to RPX-7063 at 2.0A

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSISK
ChainResidueDetails
APHE80-LYS87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER84

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR170

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS335

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 257
ChainResidueDetails
ASER84electrostatic stabiliser, hydrogen bond donor
ALYS87electrostatic stabiliser, hydrogen bond donor, increase acidity
ATYR170hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU292electrostatic stabiliser, hydrogen bond acceptor
ALYS335electrostatic stabiliser, hydrogen bond donor, increase acidity
ASER338electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-29

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