3A3F

Crystal structure of penicillin binding protein 4 (dacB) from Haemophilus influenzae,complexed with novel beta-lactam (FMZ)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000270	biological_process	peptidoglycan metabolic process
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0006508	biological_process	proteolysis
A	0008360	biological_process	regulation of cell shape
A	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
B	0000270	biological_process	peptidoglycan metabolic process
B	0004185	molecular_function	serine-type carboxypeptidase activity
B	0006508	biological_process	proteolysis
B	0008360	biological_process	regulation of cell shape
B	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE FMZ A 1

Chain	Residue
A	HOH13
A	GLY422
A	SER423
A	LEU424
A	ALA68
A	SER69
A	ASP162
A	PHE167
A	SER310
A	ASN312
A	LEU362
A	THR421

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FMZ B 1

Chain	Residue
B	ALA68
B	SER69
B	ASP162
B	PHE167
B	SER310
B	ASN312
B	LEU362
B	THR421
B	GLY422
B	SER423
B	HOH484

---