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1NJ4

Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 1.9 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0004180molecular_functioncarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042803molecular_functionprotein homodimerization activity
A0051301biological_processcell division
A0071555biological_processcell wall organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER44

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALYS47

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
ASER110

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS213

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ASER44
ALYS47
AGLN148
ASER110

229380

PDB entries from 2024-12-25

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