5LOQ

Structure of coproheme bound HemQ 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	7
Details	binding site for residue NA A 301

Chain	Residue
A	ILE63
A	LEU64
A	GLY65
A	ALA68
A	ASP69
A	HOH401
B	GLU86

---

site_id	AC2
Number of Residues	22
Details	binding site for residue FEC A 302

Chain	Residue
A	TYR113
A	ARG133
A	TYR147
A	MET149
A	LYS151
A	TRP159
A	HIS174
A	GLY178
A	ARG179
A	VAL185
A	GLN186
A	GLN187
A	TRP200
A	ILE215
A	MET219
A	SER225
A	PHE231
A	HOH425
A	HOH442
A	HOH477
A	LEU110
A	SER111

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MPD A 303

Chain	Residue
A	ASN83
A	ASN87
C	SER62
C	GLN244
C	LYS247
C	LEU248

---

site_id	AC4
Number of Residues	6
Details	binding site for residue NA B 301

Chain	Residue
B	ILE63
B	LEU64
B	GLY65
B	ALA68
B	HOH410
E	GLU86

---

site_id	AC5
Number of Residues	21
Details	binding site for residue FEC B 302

Chain	Residue
B	GLU109
B	LEU110
B	SER111
B	ARG133
B	TYR147
B	MET149
B	TRP159
B	HIS174
B	GLY178
B	TYR181
B	ALA182
B	VAL185
B	GLN187
B	TRP200
B	VAL202
B	LEU204
B	ILE215
B	MET219
B	SER225
B	PHE231
B	HOH403

---

site_id	AC6
Number of Residues	5
Details	binding site for residue MPD B 303

Chain	Residue
A	LEU248
B	GLU80
B	ASN83
B	ASN87
B	HOH401

---

site_id	AC7
Number of Residues	6
Details	binding site for residue NA C 301

Chain	Residue
A	GLU86
C	ILE63
C	LEU64
C	GLY65
C	ALA68
C	HOH406

---

site_id	AC8
Number of Residues	22
Details	binding site for residue FEC C 302

Chain	Residue
C	SER111
C	ASN112
C	TYR113
C	TYR147
C	MET149
C	TRP159
C	ILE171
C	HIS174
C	GLY178
C	ARG179
C	TYR181
C	ALA182
C	VAL185
C	GLN187
C	TRP200
C	ILE215
C	MET219
C	SER225
C	PHE231
C	HOH403
C	HOH410
C	HOH453

---

site_id	AC9
Number of Residues	6
Details	binding site for residue NA D 301

Chain	Residue
D	ALA68
D	HOH424
C	GLU86
D	ILE63
D	LEU64
D	GLY65

---

site_id	AD1
Number of Residues	26
Details	binding site for residue FEC D 302

Chain	Residue
D	SER111
D	TYR113
D	LEU114
D	ARG133
D	TYR147
D	MET149
D	LYS151
D	TRP159
D	ILE171
D	HIS174
D	GLY178
D	ARG179
D	VAL185
D	GLN186
D	GLN187
D	TRP200
D	ILE215
D	VAL216
D	MET219
D	SER225
D	PHE231
D	HOH404
D	HOH406
D	HOH422
D	HOH454
D	HOH484

---

site_id	AD2
Number of Residues	3
Details	binding site for residue MPD D 303

Chain	Residue
C	ASN87
D	GLN244
D	LYS247

---

site_id	AD3
Number of Residues	6
Details	binding site for residue NA E 301

Chain	Residue
D	GLU86
E	ILE63
E	LEU64
E	GLY65
E	ALA68
E	HOH415

---

site_id	AD4
Number of Residues	20
Details	binding site for residue FEC E 302

Chain	Residue
E	SER111
E	TYR113
E	TYR147
E	MET149
E	TRP159
E	HIS174
E	GLY178
E	ARG179
E	TYR181
E	ALA182
E	VAL185
E	GLN187
E	TRP200
E	ILE215
E	MET219
E	SER225
E	PHE231
E	HOH402
E	HOH417
E	HOH469

---

site_id	AD5
Number of Residues	6
Details	binding site for residue MPD E 303

Chain	Residue
B	GLN244
B	LEU248
E	GLU84
E	ASN87
E	HOH414
E	HOH448

---

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

---