3IQ6

Crystal structure of a tetrameric Zn-bound cytochrome cb562 complex with covalently and non-covalently stabilized interfaces

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0005506	molecular_function	iron ion binding
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0022900	biological_process	electron transport chain
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
D	0005506	molecular_function	iron ion binding
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0022900	biological_process	electron transport chain
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0009055	molecular_function	electron transfer activity
E	0020037	molecular_function	heme binding
E	0022900	biological_process	electron transport chain
E	0042597	cellular_component	periplasmic space
E	0046872	molecular_function	metal ion binding
F	0005506	molecular_function	iron ion binding
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
F	0022900	biological_process	electron transport chain
F	0042597	cellular_component	periplasmic space
F	0046872	molecular_function	metal ion binding
G	0005506	molecular_function	iron ion binding
G	0009055	molecular_function	electron transfer activity
G	0020037	molecular_function	heme binding
G	0022900	biological_process	electron transport chain
G	0042597	cellular_component	periplasmic space
G	0046872	molecular_function	metal ion binding
H	0005506	molecular_function	iron ion binding
H	0009055	molecular_function	electron transfer activity
H	0020037	molecular_function	heme binding
H	0022900	biological_process	electron transport chain
H	0042597	cellular_component	periplasmic space
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	LEU3
A	PHE65
A	LEU68
A	CYS98
A	CYS101
A	HIS102
A	ARG106
A	GLU4
A	MET7
A	GLU8
A	LEU10
A	ASN11
A	PRO45
A	PRO46
A	PHE61

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	HIS73
A	HIS77
B	HIS63
C	ASP74

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
B	GLU4
B	MET7
B	GLU8
B	LEU10
B	ASN11
B	PRO45
B	PRO46
B	PHE61
B	CYS98
B	CYS101
B	HIS102
B	TYR105
B	ARG106
B	HOH130

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 201

Chain	Residue
A	HIS63
B	HIS73
B	HIS77
D	ASP74

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
C	GLU4
C	MET7
C	GLU8
C	LEU10
C	ASN11
C	PRO45
C	PRO46
C	PHE61
C	LEU94
C	CYS98
C	CYS101
C	HIS102
C	ARG106
C	HOH135
H	GLU49

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 201

Chain	Residue
A	ASP74
C	HIS73
C	HIS77
D	HIS63

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
D	GLU4
D	MET7
D	PRO45
D	PHE61
D	LEU94
D	CYS98
D	CYS101
D	HIS102
D	ARG106

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 201

Chain	Residue
B	ASP74
C	HIS63
D	HIS73
D	HIS77

---

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM E 150

Chain	Residue
D	GLU49
E	GLU4
E	MET7
E	GLU8
E	LEU10
E	ASN11
E	LEU14
E	PRO45
E	PHE61
E	PHE65
E	LEU94
E	THR97
E	CYS98
E	CYS101
E	HIS102
E	ARG106

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 201

Chain	Residue
E	HIS73
E	HIS77
G	ASP74
H	HIS63

---

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM F 150

Chain	Residue
F	CYS98
F	CYS101
F	HIS102
F	ARG106
F	HOH117
C	HOH122
F	GLU4
F	MET7
F	ASN11
F	LEU14
F	PRO45
F	PRO46
F	PHE61
F	PHE65
F	LEU94

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 201

Chain	Residue
F	HIS73
F	HIS77
G	HIS63
H	ASP74

---

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM G 150

Chain	Residue
G	LEU3
G	GLU4
G	MET7
G	GLU8
G	LEU10
G	ASN11
G	PRO45
G	PRO46
G	PHE61
G	PHE65
G	LEU68
G	LEU94
G	CYS98
G	CYS101
G	HIS102
G	TYR105

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 201

Chain	Residue
E	ASP74
F	HIS63
G	HIS73
G	HIS77

---

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM H 150

Chain	Residue
H	GLU4
H	MET7
H	ASN11
H	MET33
H	PRO45
H	PRO46
H	PHE61
H	PHE65
H	LEU94
H	CYS98
H	CYS101
H	HIS102
H	ARG106

---

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 201

Chain	Residue
E	HIS63
F	ASP74
H	HIS73
H	HIS77

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: axial binding residue

Chain	Residue	Details
A	MET7
E	HIS102
F	MET7
F	HIS102
G	MET7
G	HIS102
H	MET7
H	HIS102
A	HIS102
B	MET7
B	HIS102
C	MET7
C	HIS102
D	MET7
D	HIS102
E	MET7

---