4ZPU

The structure of DLP12 endolysin exhibits likely active and inactive conformations.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0009253	biological_process	peptidoglycan catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0003824	molecular_function	catalytic activity
B	0009253	biological_process	peptidoglycan catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis
C	0003796	molecular_function	lysozyme activity
C	0003824	molecular_function	catalytic activity
C	0009253	biological_process	peptidoglycan catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0031640	biological_process	killing of cells of another organism
C	0042742	biological_process	defense response to bacterium
C	0044659	biological_process	viral release from host cell by cytolysis
D	0003796	molecular_function	lysozyme activity
D	0003824	molecular_function	catalytic activity
D	0009253	biological_process	peptidoglycan catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016998	biological_process	cell wall macromolecule catabolic process
D	0031640	biological_process	killing of cells of another organism
D	0042742	biological_process	defense response to bacterium
D	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ACT A 201

Chain	Residue
A	GLY57
A	LYS58
A	ILE60

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site_id	AC2
Number of Residues	4
Details	binding site for residue ACT B 201

Chain	Residue
B	GLY54
B	HIS55
B	THR56
B	TYR107

---

site_id	AC3
Number of Residues	6
Details	binding site for residue ACT C 201

Chain	Residue
C	LYS58
C	ASP59
C	ILE60
C	LEU62
B	TYR140
C	GLY57

---

site_id	AC4
Number of Residues	4
Details	binding site for residue FMT C 202

Chain	Residue
C	GLY54
C	HIS55
C	THR56
C	TYR107

---

site_id	AC5
Number of Residues	3
Details	binding site for residue FMT C 203

Chain	Residue
A	LYS58
C	ARG137
C	TRP138

---

site_id	AC6
Number of Residues	2
Details	binding site for residue ACT D 201

Chain	Residue
D	THR56
D	ASP78

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	GLU35
B	GLU35
C	GLU35
D	GLU35

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	ASP44
B	ASP44
C	ASP44
D	ASP44

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