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8TJ3

Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0008955molecular_functionpeptidoglycan glycosyltransferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0015648molecular_functionlipid-linked peptidoglycan transporter activity
B0015836biological_processlipid-linked peptidoglycan transport
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0031504biological_processpeptidoglycan-based cell wall organization
B0032153cellular_componentcell division site
B0051301biological_processcell division
B0071555biological_processcell wall organization
C0004180molecular_functioncarboxypeptidase activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008360biological_processregulation of cell shape
C0008658molecular_functionpenicillin binding
C0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0046677biological_processresponse to antibiotic
C0071555biological_processcell wall organization
C0071972molecular_functionpeptidoglycan L,D-transpeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00428
Number of Residues25
DetailsFTSW_RODA_SPOVE Cell cycle proteins ftsW / rodA / spoVE signature. NigmvsGIlPVvGVplpLVSYGGSA
ChainResidueDetails
BASN321-ALA345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:37620344
ChainResidueDetails
CMET378-ALA398
BTYR71-TRP74

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_02081
ChainResidueDetails
CLEU399-LEU419
BILE50-VAL70
BALA75-ILE95
BSER136-ALA156
BLEU160-SER180
BLEU183-MET203
BPHE263-LEU283
BLEU312-VAL332
BLEU336-VAL356

site_idSWS_FT_FI3
Number of Residues590
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:37620344
ChainResidueDetails
CGLN420-HIS1010

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:30995398, ECO:0000269|PubMed:3148617, ECO:0000269|PubMed:37620344
ChainResidueDetails
CSER707
BGLN157-ASP159
BHIS204-ASP262
BGLY333-PRO335

site_idSWS_FT_FI5
Number of Residues18
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:37620344
ChainResidueDetails
BPRO112-ARG130

site_idSWS_FT_FI6
Number of Residues4
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:37620344
ChainResidueDetails
BASP131-PRO135

site_idSWS_FT_FI7
Number of Residues41
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BTRP181-ARG182
BTYR284-MET311
BMET357-VAL370

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PDB entries from 2025-06-25

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