3ITA

Crystal structure of Penicillin-Binding Protein 6 (PBP6) from E. coli in acyl-enzyme complex with ampicillin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000270	biological_process	peptidoglycan metabolic process
A	0004180	molecular_function	carboxypeptidase activity
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008360	biological_process	regulation of cell shape
A	0008658	molecular_function	penicillin binding
A	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042803	molecular_function	protein homodimerization activity
A	0071555	biological_process	cell wall organization
B	0000270	biological_process	peptidoglycan metabolic process
B	0004180	molecular_function	carboxypeptidase activity
B	0005886	cellular_component	plasma membrane
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008360	biological_process	regulation of cell shape
B	0008658	molecular_function	penicillin binding
B	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0009410	biological_process	response to xenobiotic stimulus
B	0016787	molecular_function	hydrolase activity
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042803	molecular_function	protein homodimerization activity
B	0071555	biological_process	cell wall organization
C	0000270	biological_process	peptidoglycan metabolic process
C	0004180	molecular_function	carboxypeptidase activity
C	0005886	cellular_component	plasma membrane
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008360	biological_process	regulation of cell shape
C	0008658	molecular_function	penicillin binding
C	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0016787	molecular_function	hydrolase activity
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042803	molecular_function	protein homodimerization activity
C	0071555	biological_process	cell wall organization
D	0000270	biological_process	peptidoglycan metabolic process
D	0004180	molecular_function	carboxypeptidase activity
D	0005886	cellular_component	plasma membrane
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008360	biological_process	regulation of cell shape
D	0008658	molecular_function	penicillin binding
D	0009002	molecular_function	serine-type D-Ala-D-Ala carboxypeptidase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0016787	molecular_function	hydrolase activity
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042803	molecular_function	protein homodimerization activity
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AIX A 500

Chain	Residue
A	ALA39
A	SER40
A	ARG194
A	THR210
A	GLY211
A	THR212
A	ARG244
A	HOH723
A	HOH754

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 353

Chain	Residue
A	ARG242
A	HOH455
A	HOH487
B	GLU183
B	ARG190

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 353

Chain	Residue
A	ARG190
B	ARG194
B	THR210
B	GLY211
B	THR212
B	ARG244

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 354

Chain	Residue
B	GLN300
B	ASN303
B	HOH825

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 353

Chain	Residue
C	THR240
C	ARG242
C	HOH365
C	HOH366
D	TRP199

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 354

Chain	Residue
C	THR210
C	GLY211
C	THR212
C	ARG244

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 355

Chain	Residue
C	GLU183
C	TRP199
D	THR240
D	ARG242

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE AIC D 501

Chain	Residue
D	PRO264
D	PHE271
D	LEU304
D	LYS305
D	ALA306
D	HOH680

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
A	SER106
A	SER40
A	LYS43
A	GLN144

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
B	SER106
B	SER40
B	LYS43
B	GLN144

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
C	SER106
C	SER40
C	LYS43
C	GLN144

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1btl

Chain	Residue	Details
D	SER106
D	SER40
D	LYS43
D	GLN144

---