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3FWL

Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0008233molecular_functionpeptidase activity
A0008658molecular_functionpenicillin binding
A0008955molecular_functionpeptidoglycan glycosyltransferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE M0E A 901
ChainResidue
AGLU233
AALA357
ASER358
AILE359
AGLN271
ALYS274
AARG286
AGLN318
AGLU323
AVAL354
ALYS355
AGLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000305
ChainResidueDetails
AGLY64-LEU87

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor; for transglycosylase activity => ECO:0000305|PubMed:10564478
ChainResidueDetails
AGLU233

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate; for transpeptidase activity => ECO:0000269|PubMed:10564478
ChainResidueDetails
ASER510

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
ASER510

224004

PDB entries from 2024-08-21

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