4WWS

Structure of Chlorite dismutase-like Protein from Listeria monocytogenes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0006783	biological_process	heme biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0006783	biological_process	heme biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004601	molecular_function	peroxidase activity
C	0006783	biological_process	heme biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0004601	molecular_function	peroxidase activity
D	0006783	biological_process	heme biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification
E	0004601	molecular_function	peroxidase activity
E	0006783	biological_process	heme biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue K A 301

Chain	Residue
A	ILE63
A	GLY65
A	ALA68
A	ASP69
B	GLU86

---

site_id	AC2
Number of Residues	5
Details	binding site for residue K A 302

Chain	Residue
C	ASP69
A	GLU86
C	ILE63
C	GLY65
C	ALA68

---

site_id	AC3
Number of Residues	7
Details	binding site for residue K B 301

Chain	Residue
B	ILE63
B	GLY65
B	ALA68
B	ASP69
B	HOH459
E	GLU86
E	HOH434

---

site_id	AC4
Number of Residues	6
Details	binding site for residue K C 301

Chain	Residue
C	GLU86
D	ILE63
D	GLY65
D	ALA68
D	ASP69
D	HOH477

---

site_id	AC5
Number of Residues	7
Details	binding site for residue K D 301

Chain	Residue
D	GLU86
D	HOH480
E	ILE63
E	GLY65
E	ALA68
E	ASP69
E	HOH545

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305|PubMed:31423350

Chain	Residue	Details
A	TYR147
B	TYR147
C	TYR147
D	TYR147
E	TYR147

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ

Chain	Residue	Details
A	ARG133
C	TYR147
C	GLN187
C	SER225
D	ARG133
D	TYR147
D	GLN187
D	SER225
E	ARG133
E	TYR147
E	GLN187
A	TYR147
E	SER225
A	GLN187
A	SER225
B	ARG133
B	TYR147
B	GLN187
B	SER225
C	ARG133

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:27758026, ECO:0007744|PDB:5LOQ

Chain	Residue	Details
A	HIS174
B	HIS174
C	HIS174
D	HIS174
E	HIS174

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