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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_FI2
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"37620344","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"37620344","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues62
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_02081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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