Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ITB

Crystal structure of Penicillin-Binding Protein 6 (PBP6) from E. coli in complex with a substrate fragment

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0004180molecular_functioncarboxypeptidase activity
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042803molecular_functionprotein homodimerization activity
A0071555biological_processcell wall organization
B0000270biological_processpeptidoglycan metabolic process
B0004180molecular_functioncarboxypeptidase activity
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008360biological_processregulation of cell shape
B0008658molecular_functionpenicillin binding
B0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0009410biological_processresponse to xenobiotic stimulus
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042803molecular_functionprotein homodimerization activity
B0071555biological_processcell wall organization
C0000270biological_processpeptidoglycan metabolic process
C0004180molecular_functioncarboxypeptidase activity
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
C0009410biological_processresponse to xenobiotic stimulus
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042803molecular_functionprotein homodimerization activity
C0071555biological_processcell wall organization
D0000270biological_processpeptidoglycan metabolic process
D0004180molecular_functioncarboxypeptidase activity
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008360biological_processregulation of cell shape
D0008658molecular_functionpenicillin binding
D0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0009410biological_processresponse to xenobiotic stimulus
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042803molecular_functionprotein homodimerization activity
D0071555biological_processcell wall organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000250
ChainResidueDetails
ASER40
BSER40
CSER40
DSER40

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS43
BLYS43
CLYS43
DLYS43

site_idSWS_FT_FI3
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ASER106
BSER106
CSER106
DSER106

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS209
BLYS209
CLYS209
DLYS209

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
ASER106
ASER40
ALYS43
AGLN144

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
BSER106
BSER40
BLYS43
BGLN144

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
CSER106
CSER40
CLYS43
CGLN144

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
DSER106
DSER40
DLYS43
DGLN144

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon